ATPG_SALTY
ID ATPG_SALTY Reviewed; 287 AA.
AC Q8ZKW8; Q9RFL4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=STM3866;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=TA98;
RA Kim H.-K., Heo N.-J., Ghim S.-Y., Song B.-H.;
RT "Molecular structure of nonacistronic atp genes encoding ATP synthase in
RT Salmonella typhimurium.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00815}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC 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; AF188265; AAF19361.1; -; mRNA.
DR EMBL; AE006468; AAL22724.1; -; Genomic_DNA.
DR RefSeq; NP_462765.1; NC_003197.2.
DR RefSeq; WP_000896506.1; NC_003197.2.
DR AlphaFoldDB; Q8ZKW8; -.
DR SMR; Q8ZKW8; -.
DR STRING; 99287.STM3866; -.
DR PaxDb; Q8ZKW8; -.
DR EnsemblBacteria; AAL22724; AAL22724; STM3866.
DR GeneID; 1255393; -.
DR GeneID; 66758155; -.
DR KEGG; stm:STM3866; -.
DR PATRIC; fig|99287.12.peg.4095; -.
DR HOGENOM; CLU_050669_0_1_6; -.
DR OMA; MQITSAM; -.
DR PhylomeDB; Q8ZKW8; -.
DR BioCyc; SENT99287:STM3866-MON; -.
DR Proteomes; UP000001014; 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); IBA:GO_Central.
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:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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 2: Evidence at transcript level;
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_0000073368"
FT CONFLICT 58
FT /note="N -> H (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
FT CONFLICT 70
FT /note="E -> D (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
FT CONFLICT 102
FT /note="D -> E (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..107
FT /note="AWS -> TWT (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
FT CONFLICT 114
FT /note="E -> D (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="N -> D (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="T -> S (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
FT CONFLICT 195
FT /note="E -> D (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
FT CONFLICT 201..203
FT /note="RKA -> HKS (in Ref. 1; AAF19361)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 287 AA; 31555 MW; C33B55F0F5E4FA29 CRC64;
MAGAKEIRSK IASVQNTQKI TKAMEMVAAS KMRKSQDRMA ASRPYAETMR KVIGHLANGN
LEYKHPYLEE RDVKRVGYLV VSTDRGLCGG LNINLFKKLL ADMKAWSDKG VQCELAMIGS
KGVSFFNSVG GNVVAQVTGM GDNPSLSELI GPVKVMLQAY DEGRLDKLYI VSNKFINTMS
QVPTITQLLP LPASEDDDLK RKAWDYLYEP DPKALLDTLL RRYVESQVYQ GVVENLASEQ
AARMVAMKAA TDNGGSLIKE LQLVYNKARQ ASITQELTEI VSGAAAV
