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Database: UniProt
Entry: C5E8S2_BIFLI
LinkDB: C5E8S2_BIFLI
Original site: C5E8S2_BIFLI 
ID   C5E8S2_BIFLI            Unreviewed;       280 AA.
AC   C5E8S2;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 60.
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   ECO:0000313|EMBL:EEQ54416.1};
GN   ORFNames=BLIG_00366 {ECO:0000313|EMBL:EEQ54416.1};
OS   Bifidobacterium longum subsp. infantis CCUG 52486.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=537937 {ECO:0000313|EMBL:EEQ54416.1};
RN   [1] {ECO:0000313|EMBL:EEQ54416.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG 52486 {ECO:0000313|EMBL:EEQ54416.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Gougoulias C., Tuohy K.M., Gibson G.R., Ward D., Mehta T., Young S.,
RA   Jaffe D., Gnerre S., Berlin A., Heiman D., Hepburn T., Shea T., Sykes S.,
RA   Alvarado L., Kodira C., Borodovsky M., Lander E., Galagan J., Nusbaum C.,
RA   Birren B.;
RT   "Annotation of Bifidobacterium longum subsp. infantis CCUG 52486.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; DS990238; EEQ54416.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5E8S2; -.
DR   HOGENOM; CLU_088880_0_0_11; -.
DR   Proteomes; UP000005084; 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   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:SF22; ATP SYNTHASE SUBUNIT DELTA, CHLOROPLASTIC; 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|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:EEQ54416.1};
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}.
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   280 AA;  31695 MW;  6796A3AF922792C3 CRC64;
     MTMRGEASRI ADRESRDSLA PKLRDTREDA WRIGNELFTI TKVLDDSIQL ERALTDPSRP
     VADKVAVLKE LLGDNAHPMT MEIMTDLVSR RWSRARDIAN AVEDFGVDAM MYYADATDAT
     LQVSIELSEL HSALLNLPVV RAKLYDYQAT SEARVKLFRE VFSGKTLNKV TMRLAEHATC
     NLRRRRYLET IQWLINKFSR HMGESMVTVT TATPLKKEQI KRLVEVYSAK VGRQVHINSV
     VDPTVLGGMR IQVGDEVTDN TVVAQLQNLH RKVQTEATPA
//
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