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Database: UniProt
Entry: D6ZXW2_BIFLJ
LinkDB: D6ZXW2_BIFLJ
Original site: D6ZXW2_BIFLJ 
ID   D6ZXW2_BIFLJ            Unreviewed;       278 AA.
AC   D6ZXW2;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 61.
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   OrderedLocusNames=BLJ_0272 {ECO:0000313|EMBL:ADG99758.1};
OS   Bifidobacterium longum subsp. longum (strain JDM301).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=759350 {ECO:0000313|EMBL:ADG99758.1, ECO:0000313|Proteomes:UP000006740};
RN   [1] {ECO:0000313|EMBL:ADG99758.1, ECO:0000313|Proteomes:UP000006740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JDM301 {ECO:0000313|EMBL:ADG99758.1,
RC   ECO:0000313|Proteomes:UP000006740};
RX   PubMed=20525832; DOI=10.1128/JB.00538-10;
RA   Wei Y.X., Zhang Z.Y., Liu C., Zhu Y.Z., Zhu Y.Q., Zheng H., Zhao G.P.,
RA   Wang S., Guo X.K.;
RT   "Complete genome sequence of Bifidobacterium longum JDM301.";
RL   J. Bacteriol. 192:4076-4077(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   -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC       - and F(0) - the membrane proton channel. F(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC       subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. F(1) is
CC       attached to F(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {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}.
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DR   EMBL; CP002010; ADG99758.1; -; Genomic_DNA.
DR   RefSeq; WP_007054765.1; NC_014169.1.
DR   AlphaFoldDB; D6ZXW2; -.
DR   SMR; D6ZXW2; -.
DR   GeneID; 69577496; -.
DR   KEGG; bll:BLJ_0272; -.
DR   HOGENOM; CLU_088880_0_0_11; -.
DR   Proteomes; UP000006740; 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   HAMAP; MF_01416; ATP_synth_delta_bact; 1.
DR   InterPro; IPR020781; ATPase_OSCP/d_CS.
DR   InterPro; IPR000711; ATPase_OSCP/dsu.
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   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|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   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01416}.
SQ   SEQUENCE   278 AA;  31463 MW;  B8732D18A6737800 CRC64;
     MRGEASRIAD RESRDSLAPK LRDTREDAWR IGNELFTITK VLDDSIQLER ALTDPSRPVA
     DKVAVLKELL GDNAHPMTME IMTDLVSRRW SRARDIANAV EDFGVDAMMY YADATDATLQ
     VSIELSELHS ALLNLPVVRA KLYDYQATSE ARVKLFREVF SGKTLNKVTM RLAEHATCNL
     RRRRYLETIQ WLINKFSRHM GESMVTVTTA TPLKKEQIKR LVEVYSAKVG RQVHINSVVD
     PTVLGGMRIQ VGDEVTDNTV VAQLQNLHRK VQTEATPA
//
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