Marinomonas primoryensis (CIP 108051, JCM 11775, KMM 3633)

Name: Marinomonas primoryensis (CIP 108051, JCM 11775, KMM 3633)
Creator: BacDive
License: http://creativecommons.org/licenses/by/4.0/

BacDive ID 137570

Type strain

Culture col. no. CIP 108051 JCM 11775 KMM 3633 NRIC 523 NRIC 0523 2 more

NCBI tax ID(s) 178399

Special Collections JCM CIP

History M. Uchino <-- KMM 3633. CIP <- 2003, JCM <- 2002, M. Uchino <- KMM

Links

Marinomonas primoryensis CIP 108051 is a Gram-negative, rod-shaped bacterium of the family Oceanospirillaceae.

Gram-negative rod-shaped genome sequence 16S sequence Bacteria

Name and taxonomic classification

SI-ID 88299

JCM11775,CIP 108051,IAM 15010,NBRC 103029

@ref 20215

Last LPSN update 2026-02-09 11:32:55

Domain Bacteria

Phylum Pseudomonadota

Class Gammaproteobacteria

Order Oceanospirillales

Family Oceanospirillaceae

Genus Marinomonas

Species Marinomonas primoryensis

Full scientific name Marinomonas primoryensis Romanenko et al. 2003

BacDive ID	Other strains from **Marinomonas primoryensis** (1)	Type strain
161186	M. primoryensis JCM 11776, IAM 15011, KMM 3634

Morphology

Cell morphology

@ref	Gram stain	Cell shape	Motility
38253	negative	rod-shaped

Culture and growth conditions

Culture medium

@ref	Name	Composition	Medium link
38253	Marine agar (MA)	Distilled water make up to (1000.000 ml);Marine agar (55.100 g)
38253	CIP Medium 13		Medium recipe at CIP
38253	CIP Medium 186		Medium recipe at CIP

Culture temp

@ref	Growth	Type	Temperature (°C)
38253	positive	growth	20
38253	positive	growth	5-30
38253	negative	growth	37
38253	negative	growth	41
67770	positive	growth	30

Physiology and metabolism

Halophily

@ref	Salt	Growth	Tested relation	Concentration
38253	NaCl	positive	growth	0-6 %
38253	NaCl		growth	8 %
38253	NaCl		growth	10 %

Metabolite utilization

@ref	Chebi-ID	Metabolite	Utilization activity	Kind of utilization tested
38253	16947 ChEBI	citrate	-	carbon source
38253	4853 ChEBI	esculin	-	hydrolysis
38253	17632 ChEBI	nitrate	-	reduction
38253	16301 ChEBI	nitrite	-	reduction

Antibiotic resistance

@ref	Metabolite	Is sensitive	Is resistant
38253	0129 (2,4-Diamino-6,7-di-iso-propylpteridine phosphate)

Metabolite production

@ref	Chebi-ID	Metabolite	Production
38253	35581 ChEBI	indole

Enzymes

@ref	Value	Activity	Ec
68382	acid phosphatase	+	3.1.3.2	from API zym
38253	alcohol dehydrogenase	-	1.1.1.1
68382	alkaline phosphatase	+	3.1.3.1	from API zym
68382	alpha-chymotrypsin	-	3.4.21.1	from API zym
68382	alpha-fucosidase	-	3.2.1.51	from API zym
68382	alpha-galactosidase	-	3.2.1.22	from API zym
68382	alpha-glucosidase	+	3.2.1.20	from API zym
68382	alpha-mannosidase	-	3.2.1.24	from API zym
38253	amylase	-
68382	beta-galactosidase	-	3.2.1.23	from API zym
38253	beta-galactosidase	+	3.2.1.23
68382	beta-glucosidase	-	3.2.1.21	from API zym
68382	beta-glucuronidase	-	3.2.1.31	from API zym
38253	caseinase	-	3.4.21.50
38253	catalase	+	1.11.1.6
68382	cystine arylamidase	-	3.4.11.3	from API zym
68382	esterase (C 4)	+		from API zym
68382	esterase lipase (C 8)	+		from API zym
38253	gelatinase	-
38253	lecithinase	-
68382	leucine arylamidase	+	3.4.11.1	from API zym
38253	lipase	-
68382	lipase (C 14)	-		from API zym
38253	lysine decarboxylase	-	4.1.1.18
68382	N-acetyl-beta-glucosaminidase	-	3.2.1.52	from API zym
68382	naphthol-AS-BI-phosphohydrolase	+		from API zym
38253	ornithine decarboxylase	-	4.1.1.17
38253	oxidase	+
38253	protease	-
68382	trypsin	-	3.4.21.4	from API zym
38253	tryptophan deaminase	-
38253	tween esterase	-
38253	urease	-	3.5.1.5
68382	valine arylamidase	-		from API zym

API zym

@ref	Control	Alkaline phosphatase	Esterase (C 4)	2-naphtyl caprylateEsterase Lipase (C 8)	Lipase (C 14)	L-leucyl-2-naphthylamideLeucine arylamidase	L-valyl-2-naphthylamideValine arylamidase	L-cystyl-2-naphthylamideCystine arylamidase	Trypsin	alpha- Chymotrypsin	Acid phosphatase	Naphthol-AS-BI-phosphateNaphthol-AS-BI-phosphohydrolase	alpha- Galactosidase	beta- Galactosidase	beta- Glucuronidase	alpha- Glucosidase	beta- Glucosidase	N-acetyl-beta- glucosaminidase	alpha- Mannosidase	alpha- Fucosidase
38253	+	+	+	+	-	+	-	-	-	-	+	+	-	-	-	+	-	-	-	-

API biotype100

@ref	ControlQ	D-glucose as carbon sourceGLU	D-fructose as carbon sourceFRU	D-galactose as carbon sourceGAL	D-trehalose as carbon sourceTRE	D-mannose as carbon sourceMNE	L-sorbose as carbon sourceSBE	D-melibiose as carbon sourceMEL	sucrose as carbon sourceSAC	D-raffinose as carbon sourceRAF	maltotriose as carbon sourceMTE	maltose as carbon sourceMAL	lactose as carbon sourceLAC	lactulose as carbon sourceLTE	1-O-methyl-beta-galactopyranoside as carbon sourceMbGa	1-O-methyl-alpha-galactopyranoside as carbon sourceMaGa	D-cellobiose as carbon sourceCEL	gentiobiose as carbon sourceGEN	1-O-methyl-beta-D-glucopyranoside as carbon sourceMbGu	esculin as carbon sourceESC	D-ribose as carbon sourceRIB	L-arabinose as carbon sourceARA	D-xylose as carbon sourceXYL	palatinose as carbon sourcePLE	L-rhamnose as carbon sourceRHA	L-fucose as carbon sourceFUC	D-melezitose as carbon sourceMLZ	D-arabitol as carbon sourceDARL	L-arabitol as carbon sourceLARL	xylitol as carbon sourceXLT	dulcitol as carbon sourceDUL	D-tagatose as carbon sourceTAG	glycerol as carbon sourceGLY	myo-inositol as carbon sourceINO	D-mannitol as carbon sourceMAN	maltitol as carbon sourceMTL	D-turanose as carbon sourceTUR	D-sorbitol as carbon sourceSOR	adonitol as carbon sourceADO	hydroxyquinoline-beta-glucuronide as carbon sourceHBG	D-lyxose as carbon sourceLYX	i-erythritol as carbon sourceERY	1-O-methyl-alpha-D-glucoside as carbon sourceMDG	3-O-methyl-D-glucose as carbon source3MDG	D-saccharate as carbon sourceSAT	mucate as carbon sourceMUC	L-tartrate as carbon sourceLTAT	D-tartrate as carbon sourceDTAT	meso-tartrate as carbon sourceMTAT	D-malate as carbon sourceDMLT	L-malate as carbon sourceLMLT	cis-aconitate as carbon sourceCATE	trans-aconitate as carbon sourceTATE	tricarballylate as carbon sourceTTE	citrate as carbon sourceCIT	D-glucuronate as carbon sourceGRT	D-galacturonate as carbon sourceGAT	2-ketogluconate as carbon source2KG	5-ketogluconate as carbon source5KG	tryptophan as carbon sourceTRY	N-acetyl-D-glucosamine as carbon sourceNAG	D-gluconate as carbon sourceGNT	phenylacetate as carbon sourcePAC	protocatechuate as carbon sourcePAT	4-hydroxybenzoate as carbon sourcepOBE	quinate as carbon sourceQAT	gentisate as carbon sourceGTE	3-hydroxybenzoate as carbon sourcemOBE	benzoate as carbon sourceBAT	3-phenylpropionate as carbon sourcePPAT	m-coumarate as carbon sourceCMT	trigonelline as carbon sourceTGE	betaine as carbon sourceBET	putrescine as carbon sourcePCE	4-aminobutyrate as carbon sourceABT	histamine as carbon sourceHIN	DL-lactate as carbon sourceLAT	caprate as carbon sourceCAP	caprylate as carbon sourceCYT	L-histidine as carbon sourceHIS	succinate as carbon sourceSUC	fumarate as carbon sourceFUM	glutarate as carbon sourceGRE	DL-glycerate as carbon sourceGYT	5-aminovalerate as carbon sourceAVT	ethanolamine as carbon sourceETN	tryptamine as carbon sourceTTN	D-glucosamine as carbon sourceGLN	itaconate as carbon sourceITA	3-hydroxybutyrate as carbon source3OBU	L-aspartate as carbon sourceAPT	L-glutamate as carbon sourceGTT	L-proline as carbon sourcePRO	D-alanine as carbon sourceDALA	L-alanine as carbon sourceLALA	L-serine as carbon sourceSER	malonate as carbon sourceMNT	propionate as carbon sourcePROP	L-tyrosine as carbon sourceTYR	2-ketoglutarate as carbon source2KT
38253	not determinedn.d.	-	+	-	+	-	-	-	+	-	-	+	-	+	-	-	+	-	-	-	-	-	+	-	-	-	-	-	-	-	-	-	+	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	-	+	+	-	-	-	-	-	-	-	+	-	+	-	-	-	-	-	-	-	-	-	-	-	-	-	+	+	-	-	+	+	+	-	+	-	-	-	-	-	+	-	-	+	-	-	-	-	-	-	-

Isolation, sampling and environmental information

Isolation

@ref	Sample type	Geographic location	Country	Country ISO 3 Code	Continent
38253			Japan	JPN	Asia
67770	Coastal sea-ice in Amursky Bay of the Sea of Japan	near Vladivostok	Russia	RUS
38253	Environment, Coastal sea-ice in the Sea of Japan		Japan	JPN	Asia

Taxonmaps

69479

Global distribution of 16S sequence LC507445 (>99% sequence identity) for Marinomonas primoryensis subclade from Microbeatlas

Aquatic Samples	1313
Soil Samples	61
Animal Samples	346
Plant Samples	12
Total Samples	1732

Interaction and safety

Risk assessment

@ref	Biosafety level	Biosafety level comment
38253	1	Risk group (French classification)

Sequence information

Genome sequences

@ref	Description	Assembly level	INSDC accession	NCBI tax ID	Score
124043	ASM3952287v1 assembly for Marinomonas primoryensis JCM 11775	contig	GCA_039522875	178399	67.67

16S sequences

@ref	Description	Accession	Length	NCBI tax ID
67770	Marinomonas primoryensis gene for 16S ribosomal RNA, partial sequence, strain:KMM 3633	AB074193	1419	178399
67770	Marinomonas primoryensis JCM 11775 gene for 16S ribosomal RNA, partial sequence	LC507445	1463	178399
124043	Marinomonas primoryensis gene for 16S rRNA, partial sequence, strain: NBRC 103029.	AB681909	1466	178399

GC content

@ref	GC-content (mol%)	Method
67770	45.3-45.6	thermal denaturation, midpoint method (Tm)

Genome-based predictions

Literature

Topic	Title	Authors	Journal	DOI	Year
	Development of Low-Immunogenic AFPs for Cell Cryopreservation by Hydrophilic Modification.	Shen F, Jiang X, Zhu AB, Yang H, Zhang X, Zhang L.	Langmuir	10.1021/acs.langmuir.5c02398	2025
	Mechanistic Insights into the Folding Mechanism of Region V in Ice-Binding Protein Secreted by Marinomonas primoryensis Revealed by Single-Molecule Force Spectroscopy.	Wang H, Miao X, Zhai C, Chen Y, Lin Z, Zhou X, Guo M, Chai Z, Wang R, Shen W, Li H, Hu C.	Langmuir	10.1021/acs.langmuir.3c02257	2023
	The effect of temperature and nitrogen source modulation on Pseudomonas fluorescens AQP671 ice recrystallization inhibition activity.	Luhila O, Nisamedtinov I, Paalme T, Laos K, Olspert A.	PLoS One	10.1371/journal.pone.0333261	2025
	Effect of pH on the activity of ice-binding protein from Marinomonas primoryensis.	Delesky EA, Thomas PE, Charrier M, Cameron JC, Srubar WV.	Extremophiles	10.1007/s00792-020-01206-9	2021
	Non-specific porins of Gram-negative bacteria as proteins containing intrinsically disordered regions with amyloidogenic potential.	Novikova OD, Uversky VN, Zelepuga EA.	Prog Mol Biol Transl Sci	10.1016/bs.pmbts.2021.06.012	2021
	A peptide-binding domain shared with an Antarctic bacterium facilitates Vibrio cholerae human cell binding and intestinal colonization.	Lloyd CJ, Guo S, Kinrade B, Zahiri H, Eves R, Ali SK, Yildiz F, Voets IK, Davies PL, Klose KE.	Proc Natl Acad Sci U S A	10.1073/pnas.2308238120	2023
Enzymology	Bacterial sugar-binding protein as a one-step affinity purification tag on dextran-containing resins.	Kinrade B, Davies PL, Vance TDR.	Protein Expr Purif	10.1016/j.pep.2019.105564	2020
	Architectural dissection of adhesive bacterial cell surface appendages from a "molecular machines" viewpoint.	Smith OER, Bharat TAM.	J Bacteriol	10.1128/jb.00290-24	2024
Metabolism	Exploring the Effects of Subfreezing Temperature and Salt Concentration on Ice Growth Inhibition of Antarctic Gram-Negative Bacterium Marinomonas Primoryensis Using Coarse-Grained Simulation.	Nguyen H, Dac Van T, Tran N, Le L.	Appl Biochem Biotechnol	10.1007/s12010-015-1966-7	2016
	In Silico Approach Gives Insights into Ig-like Fold Containing Proteins in Vibrio parahaemolyticus: A Focus on the Fibrillar Adhesins.	Wang D, Wang H.	Toxins (Basel)	10.3390/toxins14020133	2022
	Conserved structural features anchor biofilm-associated RTX-adhesins to the outer membrane of bacteria.	Guo S, Langelaan DN, Phippen SW, Smith SP, Voets IK, Davies PL.	FEBS J	10.1111/febs.14441	2018
	Domain structure and cross-linking in a giant adhesin from the Mobiluncus mulieris bacterium.	Young PG, Paynter JM, Wardega JK, Middleditch MJ, Payne LS, Baker EN, Squire CJ.	Acta Crystallogr D Struct Biol	10.1107/s2059798323007507	2023
Metabolism	Putting life on ice: bacteria that bind to frozen water.	Bar Dolev M, Bernheim R, Guo S, Davies PL, Braslavsky I.	J R Soc Interface	10.1098/rsif.2016.0210	2016
	Aeromonas hydrophila RTX adhesin has three ligand-binding domains that give the bacterium the potential to adhere to and aggregate a wide variety of cell types.	Ye Q, Eves R, Vance TDR, Hansen T, Sage AP, Petkovic A, Bradley B, Escobedo C, Graham LA, Allingham JS, Davies PL.	mBio	10.1128/mbio.03158-24	2025
Metabolism	Structural Basis of Ligand Selectivity by a Bacterial Adhesin Lectin Involved in Multispecies Biofilm Formation.	Guo S, Vance TDR, Zahiri H, Eves R, Stevens C, Hehemann JH, Vidal-Melgosa S, Davies PL.	mBio	10.1128/mbio.00130-21	2021
	Bioinspired Threonine-Based Polymers with Potent Ice Recrystallization Inhibition Activity.	Delesky EA, Garcia LF, Lobo AJ, Mikofsky RA, Dowdy ND, Wallat JD, Miyake GM, Srubar WV.	ACS Appl Polym Mater	10.1021/acsapm.2c01496	2022
Metabolism	Engineered Living Materials Based on Adhesin-Mediated Trapping of Programmable Cells.	Guo S, Dubuc E, Rave Y, Verhagen M, Twisk SAE, van der Hek T, Oerlemans GJM, van den Oetelaar MCM, van Hazendonk LS, Bruls M, Eijkens BV, Joostens PL, Keij SR, Xing W, Nijs M, Stalpers J, Sharma M, Gerth M, Boonen RJEA, Verduin K, Merkx M, Voets IK, de Greef TFA.	ACS Synth Biol	10.1021/acssynbio.9b00404	2020
	Essential role of calcium in extending RTX adhesins to their target.	Vance TDR, Ye Q, Conroy B, Davies PL.	J Struct Biol X	10.1016/j.yjsbx.2020.100036	2020
	Dynamic Metal-Coordinated Adhesive and Self-Healable Antifreezing Hydrogels for Strain Sensing, Flexible Supercapacitors, and EMI Shielding Applications.	Ghosh A, Kumar S, Singh PP, Nandi S, Mandal M, Pradhan D, Khatua BB, Das RK.	ACS Omega	10.1021/acsomega.4c04851	2024
	Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis.	Hansen EB, Marcatili P.	Front Bioeng Biotechnol	10.3389/fbioe.2020.613986	2020
Pathogenicity	Sugar-binding and split domain combinations in repeats-in-toxin adhesins from Vibrio cholerae and Aeromonas veronii mediate cell-surface recognition and hemolytic activities.	Sherik M, Eves R, Guo S, Lloyd CJ, Klose KE, Davies PL.	mBio	10.1128/mbio.02291-23	2024
	The cold adaption profiles of Pseudoalteromonas shioyasakiensis D1497 from Yap trench to cope with cold.	Duan J, Guo W.	Biotechnol Rep (Amst)	10.1016/j.btre.2021.e00689	2021
Metabolism	Structural insights of the enzymes from the chitin utilization locus of Flavobacterium johnsoniae.	Mazurkewich S, Helland R, Mackenzie A, Eijsink VGH, Pope PB, Branden G, Larsbrink J.	Sci Rep	10.1038/s41598-020-70749-w	2020
Genetics	Genetic and Structural Diversity of Prokaryotic Ice-Binding Proteins from the Central Arctic Ocean.	Winder JC, Boulton W, Salamov A, Eggers SL, Metfies K, Moulton V, Mock T.	Genes (Basel)	10.3390/genes14020363	2023
	Diversity and antagonistic activity of sea ice bacteria isolated from the sea of Japan.	Romanenko LA, Tanaka N, Uchino M, Kalinovskaya NI, Mikhailov VV.	Microbes Environ	10.1264/jsme2.23.209	2008
	Cell Density-Regulated Adhesins Contribute to Early Disease Development and Adhesion in Ralstonia solanacearum.	Carter MD, Khokhani D, Allen C.	Appl Environ Microbiol	10.1128/aem.01565-22	2023
	A Ca2+-dependent bacterial antifreeze protein domain has a novel beta-helical ice-binding fold.	Garnham CP, Gilbert JA, Hartman CP, Campbell RL, Laybourn-Parry J, Davies PL.	Biochem J	10.1042/bj20071372	2008
	Structural insight reveals SARS-CoV-2 ORF7a as an immunomodulating factor for human CD14⁺ monocytes.	Zhou Z, Huang C, Zhou Z, Huang Z, Su L, Kang S, Chen X, Chen Q, He S, Rong X, Xiao F, Chen J, Chen S.	iScience	10.1016/j.isci.2021.102187	2021
	A minimalistic cyclic ice-binding peptide from phage display.	Stevens CA, Bachtiger F, Kong XD, Abriata LA, Sosso GC, Gibson MI, Klok HA.	Nat Commun	10.1038/s41467-021-22883-w	2021
	Multiple Adaptive Strategies of Himalayan Iodobacter sp. PCH194 to High-Altitude Stresses.	Kumar V, Kashyap P, Kumar S, Thakur V, Kumar S, Singh D.	Front Microbiol	10.3389/fmicb.2022.881873	2022
Metabolism	Structure and functional analysis of a bacterial adhesin sugar-binding domain.	Vance TDR, Guo S, Assaie-Ardakany S, Conroy B, Davies PL.	PLoS One	10.1371/journal.pone.0220045	2019
	Phasing with calcium at home.	Guo S, Campbell R, Davies PL, Allingham JS.	Acta Crystallogr F Struct Biol Commun	10.1107/s2053230x19004151	2019
Metabolism	A hyperactive, Ca2+-dependent antifreeze protein in an Antarctic bacterium.	Gilbert JA, Davies PL, Laybourn-Parry J.	FEMS Microbiol Lett	10.1016/j.femsle.2005.02.022	2005
	Structural diversity of marine anti-freezing proteins, properties and potential applications: a review.	Ghalamara S, Silva S, Brazinha C, Pintado M.	Bioresour Bioprocess	10.1186/s40643-022-00494-7	2022
Metabolism	Can Halophilic and Psychrophilic Microorganisms Modify the Freezing/Melting Curve of Cold Salty Solutions? Implications for Mars Habitability.	Garcia-Descalzo L, Gil-Lozano C, Munoz-Iglesias V, Prieto-Ballesteros O, Azua-Bustos A, Fairen AG.	Astrobiology	10.1089/ast.2019.2094	2020
	LabVIEW-operated novel nanoliter osmometer for ice binding protein investigations.	Braslavsky I, Drori R.	J Vis Exp	10.3791/4189	2013
	From ice-binding proteins to bio-inspired antifreeze materials.	Voets IK.	Soft Matter	10.1039/c6sm02867e	2017
Metabolism	Ca2+-stabilized adhesin helps an Antarctic bacterium reach out and bind ice.	Vance TD, Olijve LL, Campbell RL, Voets IK, Davies PL, Guo S.	Biosci Rep	10.1042/bsr20140083	2014
Metabolism	Statistical Optimisation of Phenol Degradation and Pathway Identification through Whole Genome Sequencing of the Cold-Adapted Antarctic Bacterium, Rhodococcus sp. Strain AQ5-07.	Lee GLY, Zakaria NN, Convey P, Futamata H, Zulkharnain A, Suzuki K, Abdul Khalil K, Shaharuddin NA, Alias SA, Gonzalez-Rocha G, Ahmad SA.	Int J Mol Sci	10.3390/ijms21249363	2020
	Unusually high mechanical stability of bacterial adhesin extender domains having calcium clamps.	Oude Vrielink AS, Vance TD, de Jong AM, Davies PL, Voets IK.	PLoS One	10.1371/journal.pone.0174682	2017
	Ice-binding proteins and the applicability and limitations of the kinetic pinning model.	Chasnitsky M, Braslavsky I.	Philos Trans A Math Phys Eng Sci	10.1098/rsta.2018.0391	2019
Metabolism	Structure of a 1.5-MDa adhesin that binds its Antarctic bacterium to diatoms and ice.	Guo S, Stevens CA, Vance TDR, Olijve LLC, Graham LA, Campbell RL, Yazdi SR, Escobedo C, Bar-Dolev M, Yashunsky V, Braslavsky I, Langelaan DN, Smith SP, Allingham JS, Voets IK, Davies PL.	Sci Adv	10.1126/sciadv.1701440	2017
	Quantification and Surface Localization of the Hemolysin A Type I Secretion System at the Endogenous Level and under Conditions of Overexpression.	Beer T, Hansch S, Pfeffer K, Smits SHJ, Weidtkamp-Peters S, Schmitt L.	Appl Environ Microbiol	10.1128/aem.01896-21	2022
	Ice-Binding Protein from Shewanella frigidimarinas Inhibits Ice Crystal Growth in Highly Alkaline Solutions.	Delesky EA, Frazier SD, Wallat JD, Bannister KL, Heveran CM, Srubar WV.	Polymers (Basel)	10.3390/polym11020299	2019
Metabolism	An Ice-Binding Protein from an Antarctic Ascomycete Is Fine-Tuned to Bind to Specific Water Molecules Located in the Ice Prism Planes.	Yamauchi A, Arai T, Kondo H, Sasaki YC, Tsuda S.	Biomolecules	10.3390/biom10050759	2020
Metabolism	Calcium-Binding Generates the Semi-Clathrate Waters on a Type II Antifreeze Protein to Adsorb onto an Ice Crystal Surface.	Arai T, Nishimiya Y, Ohyama Y, Kondo H, Tsuda S.	Biomolecules	10.3390/biom9050162	2019
	Determining the ice-binding planes of antifreeze proteins by fluorescence-based ice plane affinity.	Basu K, Garnham CP, Nishimiya Y, Tsuda S, Braslavsky I, Davies P.	J Vis Exp	10.3791/51185	2014
	Novel dimeric beta-helical model of an ice nucleation protein with bridged active sites.	Garnham CP, Campbell RL, Walker VK, Davies PL.	BMC Struct Biol	10.1186/1472-6807-11-36	2011
	Entrapment of probiotics in water extractable arabinoxylan gels: rheological and microstructural characterization.	Morales-Ortega A, Carvajal-Millan E, Brown-Bojorquez F, Rascon-Chu A, Torres-Chavez P, Lopez-Franco YL, Lizardi-Mendoza J, Martinez-Lopez AL, Campa-Mada AC.	Molecules	10.3390/molecules19033628	2014
	Water-organizing motif continuity is critical for potent ice nucleation protein activity.	Forbes J, Bissoyi A, Eickhoff L, Reicher N, Hansen T, Bon CG, Walker VK, Koop T, Rudich Y, Braslavsky I, Davies PL.	Nat Commun	10.1038/s41467-022-32469-9	2022
	Intermolecular latency regulates the essential C-terminal signal peptidase and sortase of the Porphyromonas gingivalis type-IX secretion system.	Mizgalska D, Goulas T, Rodriguez-Banqueri A, Veillard F, Madej M, Malecka E, Szczesniak K, Ksiazek M, Widziolek M, Guevara T, Eckhard U, Sola M, Potempa J, Gomis-Ruth FX.	Proc Natl Acad Sci U S A	10.1073/pnas.2103573118	2021
	Bacterial ice crystal controlling proteins.	Lorv JS, Rose DR, Glick BR.	Scientifica (Cairo)	10.1155/2014/976895	2014
	Blp1 protein shows virulence-associated features and elicits protective immunity to Acinetobacter baumannii infection.	Skerniskyte J, Karazijaite E, Deschamps J, Krasauskas R, Armalyte J, Briandet R, Suziedeliene E.	BMC Microbiol	10.1186/s12866-019-1615-3	2019
Metabolism	Re-evaluation of a bacterial antifreeze protein as an adhesin with ice-binding activity.	Guo S, Garnham CP, Whitney JC, Graham LA, Davies PL.	PLoS One	10.1371/journal.pone.0048805	2012
Phylogeny	Sequence analysis and confirmation of the type IV pili-associated proteins PilY1, PilW and PilV in Acidithiobacillus thiooxidans.	Alfaro-Saldana E, Hernandez-Sanchez A, Patron-Soberano OA, Astello-Garcia M, Mendez-Cabanas JA, Garcia-Meza JV.	PLoS One	10.1371/journal.pone.0199854	2019
Metabolism	Characterization of microbial antifreeze protein with intermediate activity suggests that a bound-water network is essential for hyperactivity.	Khan NMU, Arai T, Tsuda S, Kondo H.	Sci Rep	10.1038/s41598-021-85559-x	2021
Metabolism	NsrA, a Predicted beta-Barrel Outer Membrane Protein Involved in Plant Signal Perception and the Control of Secondary Infection in Sinorhizobium meliloti.	Garnerone AM, Sorroche F, Zou L, Mathieu-Demaziere C, Tian CF, Masson-Boivin C, Batut J.	J Bacteriol	10.1128/jb.00019-18	2018
	Identification and Characterization of an Isoform Antifreeze Protein from the Antarctic Marine Diatom, Chaetoceros neogracile and Suggestion of the Core Region.	Kim M, Gwak Y, Jung W, Jin E.	Mar Drugs	10.3390/md15100318	2017
Transcriptome	Prophage-Related Gene VpaChn25_0724 Contributes to Cell Membrane Integrity and Growth of Vibrio parahaemolyticus CHN25.	Yang L, Wang Y, Yu P, Ren S, Zhu Z, Jin Y, Yan J, Peng X, Chen L.	Front Cell Infect Microbiol	10.3389/fcimb.2020.595709	2020
	Ice-binding proteins that accumulate on different ice crystal planes produce distinct thermal hysteresis dynamics.	Drori R, Celik Y, Davies PL, Braslavsky I.	J R Soc Interface	10.1098/rsif.2014.0526	2014
	Superheating of ice crystals in antifreeze protein solutions.	Celik Y, Graham LA, Mok YF, Bar M, Davies PL, Braslavsky I.	Proc Natl Acad Sci U S A	10.1073/pnas.0909456107	2010
Metabolism	Structure and application of antifreeze proteins from Antarctic bacteria.	Munoz PA, Marquez SL, Gonzalez-Nilo FD, Marquez-Miranda V, Blamey JM.	Microb Cell Fact	10.1186/s12934-017-0737-2	2017
	Microfluidic Cold-Finger Device for the Investigation of Ice-Binding Proteins.	Haleva L, Celik Y, Bar-Dolev M, Pertaya-Braun N, Kaner A, Davies PL, Braslavsky I.	Biophys J	10.1016/j.bpj.2016.08.003	2016
	TssI2-TsiI2 of Vibrio fluvialis VflT6SS2 delivers pesticin domain-containing periplasmic toxin and cognate immunity that modulates bacterial competitiveness.	Huang Y, Han Y, Li Z, Li X, Li Z, Liu P, Liu X, Cheng Q, Fan F, Kan B, Liang W.	Gut Microbes	10.1080/19490976.2022.2136460	2022
Metabolism	Structure of amyloid-beta (20-34) with Alzheimer's-associated isomerization at Asp23 reveals a distinct protofilament interface.	Warmack RA, Boyer DR, Zee CT, Richards LS, Sawaya MR, Cascio D, Gonen T, Eisenberg DS, Clarke SG.	Nat Commun	10.1038/s41467-019-11183-z	2019
Metabolism	Flies expand the repertoire of protein structures that bind ice.	Basu K, Graham LA, Campbell RL, Davies PL.	Proc Natl Acad Sci U S A	10.1073/pnas.1422272112	2015
	Importance of trmE for growth of the psychrophile Pseudomonas syringae at low temperatures.	Singh AK, Pindi PK, Dube S, Sundareswaran VR, Shivaji S.	Appl Environ Microbiol	10.1128/aem.01523-08	2009
	Diatom assemblages promote ice formation in large lakes.	D'souza NA, Kawarasaki Y, Gantz JD, Lee RE, Beall BF, Shtarkman YM, Kocer ZA, Rogers SO, Wildschutte H, Bullerjahn GS, McKay RM.	ISME J	10.1038/ismej.2013.49	2013
Metabolism	An N-Terminal Retention Module Anchors the Giant Adhesin LapA of Pseudomonas fluorescens at the Cell Surface: a Novel Subfamily of Type I Secretion Systems.	Smith TJ, Font ME, Kelly CM, Sondermann H, O'Toole GA.	J Bacteriol	10.1128/jb.00734-17	2018
Metabolism	Structural basis for antifreeze activity of ice-binding protein from arctic yeast.	Lee JH, Park AK, Do H, Park KS, Moh SH, Chi YM, Kim HJ.	J Biol Chem	10.1074/jbc.m111.331835	2012
	New insights into ice growth and melting modifications by antifreeze proteins.	Bar-Dolev M, Celik Y, Wettlaufer JS, Davies PL, Braslavsky I.	J R Soc Interface	10.1098/rsif.2012.0388	2012
	Helical antifreeze proteins have independently evolved in fishes on four occasions.	Graham LA, Hobbs RS, Fletcher GL, Davies PL.	PLoS One	10.1371/journal.pone.0081285	2013
	New Cysteine-Rich Ice-Binding Protein Secreted from Antarctic Microalga, Chloromonas sp.	Jung W, Campbell RL, Gwak Y, Kim JI, Davies PL, Jin E.	PLoS One	10.1371/journal.pone.0154056	2016
Metabolism	Structural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica.	Peters B, Stein J, Klingl S, Sander N, Sandmann A, Taccardi N, Sticht H, Gerlach RG, Muller YA, Hensel M.	PLoS Pathog	10.1371/journal.ppat.1006418	2017
	Metal ion-dependent, reversible, protein filament formation by designed beta-roll polypeptides.	Scotter AJ, Guo M, Tomczak MM, Daley ME, Campbell RL, Oko RJ, Bateman DA, Chakrabartty A, Sykes BD, Davies PL.	BMC Struct Biol	10.1186/1472-6807-7-63	2007
Phylogeny	Porin from Marine Bacterium Marinomonas primoryensis KMM 3633(T): Isolation, Physico-Chemical Properties, and Functional Activity.	Novikova OD, Khomenko VA, Kim NY, Likhatskaya GN, Romanenko LA, Aksenova EI, Kunda MS, Ryzhova NN, Portnyagina OY, Solov'eva TF, Voronina OL	Molecules	10.3390/molecules25143131	2020
	Psychroserpens ponticola sp. nov. and Marinomonas maritima sp. nov., isolated from seawater.	Kristyanto S, Jung J, Kim JM, Choi BJ, Han DM, Lee SC, Jeon CO.	Int J Syst Evol Microbiol	10.1099/ijsem.0.006090	2023
Phylogeny	Marinomonas transparens sp. nov. and Marinomonas sargassi sp. nov., isolated from marine alga.	Cui N, Zhang Y, Fan J, Liu X, Li Y, Zhang X, Guan J, Li T, Wang Y.	Int J Syst Evol Microbiol	10.1099/ijsem.0.005879	2023
	Paracoccus broussonetiae subsp. drimophilus subsp. nov., a Novel Subspecies Salt-Tolerant Endophytic Bacterium from Maize Root in Hunan.	Li X, Zhou C, Li M, Zhang Q, Su L, Li X.	Life (Basel)	10.3390/life15030354	2025
Phylogeny	Marinomonas polaris sp. nov., a psychrohalotolerant strain isolated from coastal sea water off the subantarctic Kerguelen islands.	Gupta P, Chaturvedi P, Pradhan S, Delille D, Shivaji S.	Int J Syst Evol Microbiol	10.1099/ijs.0.63921-0	2006
Phylogeny	Marinomonas pontica sp. nov., isolated from the Black Sea.	Ivanova EP, Onyshchenko OM, Christen R, Lysenko AM, Zhukova NV, Shevchenko LS, Kiprianova EA.	Int J Syst Evol Microbiol	10.1099/ijs.0.63326-0	2005
Phylogeny	Marinomonas ushuaiensis sp. nov., isolated from coastal sea water in Ushuaia, Argentina, sub-Antarctica.	Prabagaran SR, Suresh K, Manorama R, Delille D, Shivaji S	Int J Syst Evol Microbiol	10.1099/ijs.0.63363-0	2005
Phylogeny	Marinomonas flavescens sp. nov., isolated from seawater adjacent to Fildes Peninsula, Antarctica.	Hu M, Zhai Y, Zhang Y, Han X, Fang W, Fang Z, Xiao Y	Int J Syst Evol Microbiol	10.1099/ijsem.0.003631	2019
Phylogeny	Marinomonas primoryensis sp. nov., a novel psychrophile isolated from coastal sea-ice in the Sea of Japan.	Romanenko LA, Uchino M, Mikhailov VV, Zhukova NV, Uchimura T	Int J Syst Evol Microbiol	10.1099/ijs.0.02280-0	2003

References

#20215	Parte, A.C., Sardà Carbasse, J., Meier-Kolthoff, J.P., Reimer, L.C. and Göker, M.: List of Prokaryotic names with Standing in Nomenclature (LPSN) moves to the DSMZ. IJSEM ( DOI 10.1099/ijsem.0.004332 )
#38253	Collection of Institut Pasteur ; Curators of the CIP; CIP 108051
#67770	Japan Collection of Microorganism (JCM) ; Curators of the JCM;
#68382	Automatically annotated from API zym .
#69479	João F Matias Rodrigues, Janko Tackmann,Gregor Rot, Thomas SB Schmidt, Lukas Malfertheiner, Mihai Danaila,Marija Dmitrijeva, Daniela Gaio, Nicolas Näpflin and Christian von Mering. University of Zurich.: MicrobeAtlas 1.0 beta .
#124043	Isabel Schober, Julia Koblitz: Data extracted from sequence databases, automatically matched based on designation and taxonomy .
#126262	A. Lissin, I. Schober, J. F. Witte, H. Lüken, A. Podstawka, J. Koblitz, B. Bunk, P. Dawyndt, P. Vandamme, P. de Vos, J. Overmann, L. C. Reimer: StrainInfo—the central database for linked microbial strain identifiers. ( DOI 10.1093/database/baaf059 )

Rate our new design

Content

About us

Marinomonas primoryensis (CIP 108051, JCM 11775, KMM 3633)

Name and taxonomic classification

Morphology

Cell morphology

Culture and growth conditions

Culture medium

Culture temp

Physiology and metabolism

Halophily

Metabolite utilization

Antibiotic resistance

Metabolite production

Enzymes

API zym

API biotype100

Isolation, sampling and environmental information

Isolation

Taxonmaps

Interaction and safety

Risk assessment

Sequence information

Genome sequences

Genome browser: GCA_039522875

16S sequences

GC content

Genome-based predictions

Literature

Literature

References

BacDive

Help

Social Media