ATPG_EDWI9
ID ATPG_EDWI9 Reviewed; 287 AA.
AC C5BF39;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=NT01EI_3911;
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR71022.1; -; Genomic_DNA.
DR RefSeq; WP_015873050.1; NC_012779.2.
DR AlphaFoldDB; C5BF39; -.
DR SMR; C5BF39; -.
DR STRING; 67780.B6E78_11080; -.
DR EnsemblBacteria; ACR71022; ACR71022; NT01EI_3911.
DR GeneID; 7961477; -.
DR KEGG; eic:NT01EI_3911; -.
DR PATRIC; fig|634503.3.peg.3482; -.
DR HOGENOM; CLU_050669_0_1_6; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR Proteomes; UP000001485; 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_1000213034"
SQ SEQUENCE 287 AA; 31756 MW; 4FD4842CEC91FDDC CRC64;
MAGAKEIRSK IASVQNTQKI TKAMEMVAAS KMRKTQDRMA ASRPYAETMR KVIGHLALGN
LEYKHPYLEE RDIKRVGYLV VSTDRGLCGG LNINLFKKLL TEMKEWNQKG VDIDLALIGS
KAVSFFGSVG GNVVAQVTGM GDNPSLSELI GPVKVMLQAY DEGRLDRLYV VSNKFINTMS
QEPQVIQLLP LPKADDAELK RKSWDYLYEP DPKALLDTLL RRYVESQVYQ GVVENLASEQ
AARMVAMKAA TDNGGNLIKE LQLVYNKARQ ASITQELTEI VSGAAAV
