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Database: UniProt
Entry: A8TB45_9VIBR
LinkDB: A8TB45_9VIBR
Original site: A8TB45_9VIBR 
ID   A8TB45_9VIBR            Unreviewed;       177 AA.
AC   A8TB45;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   RecName: Full=ATP synthase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE   AltName: Full=ATP synthase F(1) sector subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE   AltName: Full=F-type ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
DE            Short=F-ATPase subunit delta {ECO:0000256|HAMAP-Rule:MF_01416};
GN   Name=atpH {ECO:0000256|HAMAP-Rule:MF_01416};
GN   ORFNames=AND4_17019 {ECO:0000313|EMBL:EDP57452.1};
OS   Vibrio sp. AND4.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP57452.1, ECO:0000313|Proteomes:UP000005159};
RN   [1] {ECO:0000313|EMBL:EDP57452.1, ECO:0000313|Proteomes:UP000005159}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AND4 {ECO:0000313|EMBL:EDP57452.1,
RC   ECO:0000313|Proteomes:UP000005159};
RX   PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA   Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA   Milton D.L., Gonzalez J.M., Pinhassi J.;
RT   "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT   starvation.";
RL   PLoS Biol. 8:E1000358-E1000358(2010).
CC   -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC       of a proton or sodium gradient. F-type ATPases consist of two
CC       structural domains, F(1) containing the extramembraneous catalytic core
CC       and F(0) containing the membrane proton channel, linked together by a
CC       central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC       in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC       the central stalk subunits to proton translocation. {ECO:0000256|HAMAP-
CC       Rule:MF_01416}.
CC   -!- FUNCTION: This protein is part of the stalk that links CF(0) to CF(1).
CC       It either transmits conformational changes from CF(0) to CF(1) or is
CC       implicated in proton conduction. {ECO:0000256|HAMAP-Rule:MF_01416}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_01416}.
CC   -!- SIMILARITY: Belongs to the ATPase delta chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01416}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EDP57452.1}.
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DR   EMBL; ABGR01000036; EDP57452.1; -; Genomic_DNA.
DR   RefSeq; WP_009844211.1; NZ_ABGR01000036.1.
DR   AlphaFoldDB; A8TB45; -.
DR   OrthoDB; 9816221at2; -.
DR   Proteomes; UP000005159; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.520.20; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
DR   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR026015; ATP_synth_OSCP/delta_N_sf.
DR   InterPro; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
DR   NCBIfam; TIGR01145; ATP_synt_delta; 1.
DR   PANTHER; PTHR11910; ATP SYNTHASE DELTA CHAIN; 1.
DR   PANTHER; PTHR11910:SF1; ATP SYNTHASE SUBUNIT O, MITOCHONDRIAL; 1.
DR   Pfam; PF00213; OSCP; 1.
DR   PRINTS; PR00125; ATPASEDELTA.
DR   SUPFAM; SSF47928; N-terminal domain of the delta subunit of the F1F0-ATP synthase; 1.
DR   PROSITE; PS00389; ATPASE_DELTA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis {ECO:0000256|ARBA:ARBA00023310, ECO:0000256|HAMAP-
KW   Rule:MF_01416}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01416};
KW   CF(1) {ECO:0000256|ARBA:ARBA00023196, ECO:0000256|HAMAP-Rule:MF_01416};
KW   Hydrogen ion transport {ECO:0000256|ARBA:ARBA00022781, ECO:0000256|HAMAP-
KW   Rule:MF_01416}; Hydrolase {ECO:0000313|EMBL:EDP57452.1};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_01416};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01416};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ   SEQUENCE   177 AA;  19514 MW;  6983FBC0BF145DA7 CRC64;
     MSNLTTIARP YAKAAFDFAV DKDQLDQWGQ MLSFATEVTK NEQMKELLTG SVSADKMAEI
     FVAVCGEQVD AHGQNLIKVM AENGRLSALP DVCEQFFLLK KEHEKEIDVE VISASELSDE
     QLAKIGSKLE VRLERKVKLN CSVDETLLGG VIIRAGDLVI DDSARGRLNR LSDALQS
//
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