ATPG_BIFLO
ID ATPG_BIFLO Reviewed; 307 AA.
AC Q8G7B2;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=ATP synthase gamma chain {ECO:0000255|HAMAP-Rule:MF_00815};
DE AltName: Full=ATP synthase F1 sector gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815};
DE AltName: Full=F-ATPase gamma subunit {ECO:0000255|HAMAP-Rule:MF_00815};
GN Name=atpG {ECO:0000255|HAMAP-Rule:MF_00815}; OrderedLocusNames=BL0358;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. The gamma chain is believed to be important in
CC regulating ATPase activity and the flow of protons through the CF(0)
CC complex. {ECO:0000255|HAMAP-Rule:MF_00815}.
CC -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC subunits: a, b and c. {ECO:0000255|HAMAP-Rule:MF_00815}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00815};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00815}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00815}.
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DR EMBL; AE014295; AAN24196.1; -; Genomic_DNA.
DR RefSeq; NP_695560.1; NC_004307.2.
DR RefSeq; WP_007051479.1; NC_004307.2.
DR AlphaFoldDB; Q8G7B2; -.
DR SMR; Q8G7B2; -.
DR STRING; 206672.BL0358; -.
DR EnsemblBacteria; AAN24196; AAN24196; BL0358.
DR KEGG; blo:BL0358; -.
DR PATRIC; fig|206672.9.peg.1094; -.
DR HOGENOM; CLU_050669_0_0_11; -.
DR OMA; MQITSAM; -.
DR PhylomeDB; Q8G7B2; -.
DR Proteomes; UP000000439; 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:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IEA:UniProtKB-UniRule.
DR CDD; cd12151; F1-ATPase_gamma; 1.
DR HAMAP; MF_00815; ATP_synth_gamma_bact; 1.
DR InterPro; IPR035968; ATP_synth_F1_ATPase_gsu.
DR InterPro; IPR000131; ATP_synth_F1_gsu.
DR PANTHER; PTHR11693; PTHR11693; 1.
DR Pfam; PF00231; ATP-synt; 1.
DR PRINTS; PR00126; ATPASEGAMMA.
DR SUPFAM; SSF52943; SSF52943; 1.
DR TIGRFAMs; TIGR01146; ATPsyn_F1gamma; 1.
PE 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transport.
FT CHAIN 1..307
FT /note="ATP synthase gamma chain"
FT /id="PRO_0000073242"
SQ SEQUENCE 307 AA; 33866 MW; DD589C6FE3B81B38 CRC64;
MGSQLALKSR IRSTESLAKI FNAQEMIASS HIAKARDVAL NAKPYTDAIF DAVQALVAHT
HITHPIAVKD EKNPRVAVLA LTSDRGMAGP YTSSIIRETE SLLSRLDAAG KQPELFVYGR
RGSTYYKYRN RDIAATWEGD TDQPGVEIAE TISNTLMDAY MKPAEKGGVS ELYIVYTEFI
NMVVQKVRVL RMLPVEIVKN ETKVPDPDEE APATADVAPL YTFEPSLEKV LDAILPKYIQ
SRIHECLLTA AASETASRQN AMHTATDNAR NLIDDLTRKL NASRQASITQ ELTEIIGSAD
ALTKKEE
