ID   ATPG_SHIFL              Reviewed;         287 AA.
AC   P0ABA9; P00837; P00838;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=ATP synthase gamma chain;
DE   AltName: Full=ATP synthase F1 sector gamma subunit;
DE   AltName: Full=F-ATPase gamma subunit;
GN   Name=atpG; OrderedLocusNames=SF3813, S3955;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005674; AAN45253.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18944.1; -; Genomic_DNA.
DR   RefSeq; NP_709546.1; NC_004337.2.
DR   RefSeq; WP_000896498.1; NZ_WPGW01000050.1.
DR   AlphaFoldDB; P0ABA9; -.
DR   SMR; P0ABA9; -.
DR   STRING; 198214.SF3813; -.
DR   PRIDE; P0ABA9; -.
DR   EnsemblBacteria; AAN45253; AAN45253; SF3813.
DR   EnsemblBacteria; AAP18944; AAP18944; S3955.
DR   GeneID; 1026049; -.
DR   GeneID; 67417720; -.
DR   KEGG; sfl:SF3813; -.
DR   KEGG; sfx:S3955; -.
DR   PATRIC; fig|198214.7.peg.4500; -.
DR   HOGENOM; CLU_050669_0_1_6; -.
DR   OMA; MQITSAM; -.
DR   OrthoDB; 1701531at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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   InterPro; IPR023632; ATP_synth_F1_gsu_CS.
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.
DR   PROSITE; PS00153; ATPASE_GAMMA; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..287
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073370"
SQ   SEQUENCE   287 AA;  31577 MW;  2417A4B8FBDB8EF8 CRC64;
     MAGAKEIRSK IASVQNTQKI TKAMEMVAAS KMRKSQDRMA ASRPYAETMR KVIGHLAHGN
     LEYKHPYLED RDVKRVGYLV VSTDRGLCGG LNINLFKKLL AEMKTWTDKG VQCDLAMIGS
     KGVSFFNSVG GNVVAQVTGM GDNPSLSELI GPVKVMLQAY DEGRLDKLYI VSNKFINTMS
     QVPTISQLLP LPASDDDDLK HKSWDYLYEP DPKALLDTLL RRYVESQVYQ GVVENLASEQ
     AARMVAMKAA TDNGGSLIKE LQLVYNKARQ ASITQELTEI VSGAAAV