GVPA_DOLFA
ID GVPA_DOLFA Reviewed; 71 AA.
AC P10397; P80995;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Gas vesicle structural protein;
DE Short=GVP;
GN Name=gvpA;
OS Dolichospermum flosaquae (Anabaena flos-aquae).
OC Bacteria; Cyanobacteria; Nostocales; Aphanizomenonaceae; Dolichospermum.
OX NCBI_TaxID=1166;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-13.
RC STRAIN=CCAP 1403/13f;
RX PubMed=1527496; DOI=10.1099/00221287-138-6-1243;
RA Griffiths A.E., Walsby A.E., Hayes P.K.;
RT "The homologies of gas vesicle proteins.";
RL J. Gen. Microbiol. 138:1243-1250(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CCAP 1403/13f;
RX PubMed=9063646; DOI=10.3109/10425179709020156;
RA Kinsman R., Hayes P.K.;
RT "Genes encoding proteins homologous to halobacterial Gvps N, J, K, F and L
RT are located downstream of gvpC in the cyanobacterium Anabaena flos-aquae.";
RL DNA Seq. 7:97-106(1997).
RN [3]
RP PROTEIN SEQUENCE OF 2-71.
RC STRAIN=CCAP 1403/13f;
RX PubMed=3098234; DOI=10.1042/bj2360031;
RA Hayes P.K., Walsby A.E., Walker J.E.;
RT "Complete amino acid sequence of cyanobacterial gas-vesicle protein
RT indicates a 70-residue molecule that corresponds in size to the
RT crystallographic unit cell.";
RL Biochem. J. 236:31-36(1986).
CC -!- FUNCTION: Gas vesicles are small, hollow, gas filled protein structures
CC that are found in several microbial planktonic microorganisms. They
CC allow the positioning of the organism at the favorable depth for
CC growth. GvpA type proteins form the essential core of the structure.
CC -!- SUBCELLULAR LOCATION: Vacuole, gas vesicle membrane.
CC -!- SIMILARITY: Belongs to the gas vesicle protein type A family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M32060; AAA82497.1; -; Genomic_DNA.
DR EMBL; M32060; AAA82499.1; -; Genomic_DNA.
DR EMBL; U17109; AAA58709.1; -; Genomic_DNA.
DR EMBL; U17109; AAA58708.1; -; Genomic_DNA.
DR PIR; A23851; SVFZ.
DR AlphaFoldDB; P10397; -.
DR GO; GO:0033172; C:gas vesicle shell; IEA:UniProtKB-SubCell.
DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-KW.
DR GO; GO:0012506; C:vesicle membrane; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR HAMAP; MF_00576; Gas_vesicle_A; 1.
DR InterPro; IPR000638; Gas-vesicle_GvpA.
DR InterPro; IPR018493; Gas-vesicle_GvpA_CS.
DR Pfam; PF00741; Gas_vesicle; 1.
DR PROSITE; PS00234; GAS_VESICLE_A_1; 1.
DR PROSITE; PS00669; GAS_VESICLE_A_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Gas vesicle; Membrane; Vacuole.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1527496,
FT ECO:0000269|PubMed:3098234"
FT CHAIN 2..71
FT /note="Gas vesicle structural protein"
FT /id="PRO_0000199978"
FT CONFLICT 38
FT /note="E -> Q (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..70
FT /note="AVP -> VPA (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 71 AA; 7529 MW; 419D350E7661C359 CRC64;
MAVEKTNSSS SLAEVIDRIL DKGIVIDAWV RVSLVGIELL AIEARIVIAS VETYLKYAEA
VGLTQSAAVP A