ATPG_BLOPB
ID ATPG_BLOPB Reviewed; 288 AA.
AC Q494C4;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BPEN_007;
OS Blochmannia pennsylvanicus (strain BPEN).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=291272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPEN;
RX PubMed=16077009; DOI=10.1101/gr.3771305;
RA Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT evolutionary trends among bacterial mutualists of insects.";
RL Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ40657.1; -; Genomic_DNA.
DR RefSeq; WP_011282563.1; NC_007292.1.
DR AlphaFoldDB; Q494C4; -.
DR SMR; Q494C4; -.
DR STRING; 291272.BPEN_007; -.
DR EnsemblBacteria; AAZ40657; AAZ40657; BPEN_007.
DR KEGG; bpn:BPEN_007; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_0_1_6; -.
DR OMA; MQITSAM; -.
DR BioCyc; CBLO291272:BPEN_RS00040-MON; -.
DR Proteomes; UP000007794; 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 inner membrane; Cell membrane; CF(1);
KW Hydrogen ion transport; Ion transport; Membrane; Transport.
FT CHAIN 1..288
FT /note="ATP synthase gamma chain"
FT /id="PRO_0000073244"
SQ SEQUENCE 288 AA; 32670 MW; 689128D2998A89BD CRC64;
MSGLKEIRGK IDSIRNIQKI AKAMEMISVA KIYQTQRRML ISKPYAETIR KVIDHISSGT
LEYKHSYFLE RKIQSVGYWV VSTDRGLAGG LNINLLKTLL YDFNKWSNEG ITIRLAIIGS
KGASFLRSIK QTEIVSCVYG IGDAPKMSAL IGSVRVMLQL YDNNQIDRLY LAYNKFINTL
TQSPQILQIL PIISSKNSIL QTKYWDYLYE PDSKVLLNSL LQRYIESQVY QGVVENLASE
QSARMMAMKT ASDNGEVIIN DLKLFYNKAR QTKITEELTE IVSGASVI
