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Database: UniProt
Entry: A3HXY4_9BACT
LinkDB: A3HXY4_9BACT
Original site: A3HXY4_9BACT 
ID   A3HXY4_9BACT            Unreviewed;       187 AA.
AC   A3HXY4;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 75.
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=ALPR1_20513 {ECO:0000313|EMBL:EAZ81457.1};
OS   Algoriphagus machipongonensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=388413 {ECO:0000313|EMBL:EAZ81457.1, ECO:0000313|Proteomes:UP000003919};
RN   [1] {ECO:0000313|EMBL:EAZ81457.1, ECO:0000313|Proteomes:UP000003919}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR1 {ECO:0000313|EMBL:EAZ81457.1,
RC   ECO:0000313|Proteomes:UP000003919};
RX   PubMed=21183675; DOI=10.1128/JB.01421-10;
RA   Alegado R.A., Ferriera S., Nusbaum C., Young S.K., Zeng Q., Imamovic A.,
RA   Fairclough S.R., King N.;
RT   "Complete genome sequence of Algoriphagus sp. PR1, bacterial prey of a
RT   colony-forming choanoflagellate.";
RL   J. Bacteriol. 193:1485-1486(2011).
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:EAZ81457.1}.
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DR   EMBL; AAXU02000001; EAZ81457.1; -; Genomic_DNA.
DR   RefSeq; WP_008203277.1; NZ_CM001023.1.
DR   AlphaFoldDB; A3HXY4; -.
DR   STRING; 388413.ALPR1_20513; -.
DR   eggNOG; COG0712; Bacteria.
DR   HOGENOM; CLU_085114_4_1_10; -.
DR   OrthoDB; 9802471at2; -.
DR   Proteomes; UP000003919; Chromosome.
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: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:SF22; ATP SYNTHASE SUBUNIT DELTA, CHLOROPLASTIC; 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 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};
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   Reference proteome {ECO:0000313|Proteomes:UP000003919};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ   SEQUENCE   187 AA;  21654 MW;  B892D7D9785086C2 CRC64;
     MSNHRVASRY AKSIMELSLE KGKLEEVHKD FQKLTSMAKS NFDLVLLLKN PIVNSEKKLN
     VLKALFPEKT TQEMTLKFFE IISRKNREAI LVDVAREFEM QYNIHESIQV AEVTTTFAID
     DKQRAEFIEV VKELSGMTDV QLVEKINPEI IGGFVLKVND KQLDDSLSSK LRVLKAQFTQ
     NHYEKQY
//
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