{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P09413","uniProtkbId":"GVPC_DOLFA","entryAudit":{"firstPublicDate":"1989-07-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1989-07-01","entryVersion":83,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Dolichospermum flosaquae","commonName":"Anabaena flos-aquae","taxonId":1166,"lineage":["Bacteria","Bacillati","Cyanobacteriota","Cyanophyceae","Nostocales","Aphanizomenonaceae","Dolichospermum"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3141741"}],"value":"Gas vesicle protein C"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3141741"}],"value":"GVPc"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"3141741"}],"value":"gvpC"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1510555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16735729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7476201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8254305"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3141741"}],"value":"Confers stability, involved in shaping gas vesicles (GV), hollow, gas-filled proteinaceous nanostructures. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition (Probable) (Ref.4). The ratio of GvpA:GvpC is estimated to be 25:1 (PubMed:7476201, PubMed:8254305). GvpC strengthens the GV wall, probably by connecting several GvpA proteins in the same and/or adjacent ribs (Probable) (PubMed:1510555, PubMed:16735729, PubMed:7476201, Ref.5). Removal of GvpC by SDS reduces the critical collapse pressure (CCP) of stored gas vesicles from 0.23 Mpa to 0.08 MPa (Ref.5). Removal of GvpC by urea reduces CCP of freshly isolated GVs from 0.550 MPa to 0.190 MPa; addition of recombinant GvpC restores CCP to 0.508 MPa. As the turgor pressure in this species is usually 0.35 MPa (plus the water column pressure in its growth environment), this protein is essential for GV formation (PubMed:1510555)"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1510555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1527496"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16735729"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3141741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32661379"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7476201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8254305"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"}],"value":"Binds to the entire external surface of the gas vesicle (PubMed:1510555, PubMed:1527496, PubMed:16735729, PubMed:3141741, PubMed:32661379, PubMed:7476201, PubMed:8254305, Ref.5). Trypsin cleaves most of the expected sites in intact vesicles, suggesting all of GvpC is on the surface (PubMed:16735729)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1510555"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1527496"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3141741"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32661379"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7476201"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8254305"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.5"}],"value":"Gas vesicle","id":"SL-0125"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"Gas vesicles are abundant in low light, and collapse after exposure to high light"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"7476201"}],"value":"The tandem repeats probably bind across adjacent GvpA ribs with each repeat contacting 5 GvpA subunits, stiffening the vesicle"}],"commentType":"DOMAIN"},{"commentType":"MASS SPECTROMETRY","method":"MALDI","molWeight":21961.0,"molWeightError":0.0,"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16735729"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19002872"}],"value":"Can be used as an oxygen carrier in mammalian cell culture; addition of 1.8% GVs in the medium enhanced the maximum glucose utilization rate by about 30%. The GVs have both GvpA and GvpC"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29300010"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32661379"}],"value":"Engineered gas vesicles (GV) can be used for noninvasive imaging in bacteria and mice. Heterologous GVs with 2 copies of gvpA plus gvpC from this bacteria and the gvpR-gvpU operon from P.megaterium make GVs suitable for imaging of bacteria deep in mouse tissues (e.g. the gastrointestinal tract), or when expressed in tumor-homing bacteria, can be detected in tumors (PubMed:29300010). Can be used to make acoustic biosensors for ultrasound imaging. Insertion of a protease target site in GvpC and subsequent exposure to the protease leads to GVs that collapse at lower hydrostatic pressures; both endoproteases and processive exoproteases can be used. Controlling GvpC degradation allows controlled GV collapse and changes in ultrasound images (PubMed:32661379)"}],"commentType":"BIOTECHNOLOGY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3141741"}],"value":"Protein sequence was derived from constitutive gas vesicle producer strain CCAP 1403/13f, DNA sequence from CCAP 1403/13d, a spontaneous mutant which does not produce gas vesicles"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the gas vesicle GvpC family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"Gas vesicle protein C","featureId":"PRO_0000182663"},{"type":"Repeat","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3141741"}]},{"type":"Repeat","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3141741"}]},{"type":"Repeat","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3141741"}]},{"type":"Repeat","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3141741"}]},{"type":"Repeat","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3141741"}]},{"type":"Region","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"5 X 33 AA tandem repeats","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"3141741"}]},{"type":"Natural variant","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":3,"modifier":"EXACT"}},"description":"in strain: CCAP 1401/1","featureId":"","alternativeSequence":{"originalSequence":"S","alternativeSequences":["P"]}},{"type":"Natural variant","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"in strain: CCAP 1401/1","featureId":"","alternativeSequence":{"originalSequence":"MA","alternativeSequences":["IT"]}},{"type":"Natural variant","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"in strain: CCAP 1401/1","featureId":"","alternativeSequence":{"originalSequence":"AE","alternativeSequences":["VK"]}},{"type":"Mutagenesis","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Missing last 3 repeats, restores gas vesicle stability 70% as well as wild-type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7476201"}],"alternativeSequence":{}},{"type":"Mutagenesis","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Missing last 2 repeats, restores gas vesicle stability 80% as well as wild-type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7476201"}],"alternativeSequence":{}},{"type":"Mutagenesis","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Missing last repeat, restores gas vesicle stability 80% as well as wild-type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7476201"}],"alternativeSequence":{}}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0304","category":"Cellular component","name":"Gas vesicle"},{"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"3141741","citationType":"journal article","authors":["Hayes P.K.","Lazarus C.M.","Bees A.","Walker J.E.","Walsby A.E."],"citationCrossReferences":[{"database":"PubMed","id":"3141741"},{"database":"DOI","id":"10.1111/j.1365-2958.1988.tb00062.x"}],"title":"The protein encoded by gvpC is a minor component of gas vesicles isolated from the cyanobacteria Anabaena flos-aquae and Microcystis sp.","publicationDate":"1988","journal":"Mol. 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Gen. Microbiol.","firstPage":"1243","lastPage":"1250","volume":"138"},"referencePositions":["PROTEIN SEQUENCE OF 1-62","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"CCAP 1401/1","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"CI-110F2A43KSUVA","citationType":"journal article","authors":["Oliver R.A.","Walsby A.E."],"citationCrossReferences":[{"database":"DOI","id":"10.4319/lo.1984.29.4.0879"}],"title":"Direct evidence for the role of light-mediated gas vesicle collapse in the buoyancy regulation of Anabaena flos-aquae (cyanobacteria).","publicationDate":"1984","journal":"Limnol. Oceanogr.","firstPage":"879","lastPage":"886","volume":"29"},"referencePositions":["GAS VESICLE FUNCTION","INDUCTION"],"referenceComments":[{"value":"CCAP 1403/13f","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"CI-5DLDJVLQNRQM4","citationType":"journal article","authors":["Walsby A.E.","Hayes P.K."],"citationCrossReferences":[{"database":"DOI","id":"10.1099/00221287-134-10-2647"}],"title":"The Minor Cyanobacterial Gas Vesicle Protein, GVPc, Is Attached to the Outer Surface of the Gas Vesicle.","publicationDate":"1988","journal":"J. Gen. 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During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition. GVs are highly permeable to gas (Ref.7). GvpA forms the protein shell (PubMed:14695294, PubMed:1527496, PubMed:20858439, PubMed:22147705, PubMed:3098234, PubMed:3141741, PubMed:6409075, Ref.5). The ratio of GvpA:GvpC is estimated to be 33:1 and more recently 25:1 (PubMed:3141741, PubMed:8254305)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00576"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9172769"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"184286"}],"value":"The gas vesicle shell is 2 nm thick and consists of a single layer of this protein. 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