ATPG_EHRRG
ID ATPG_EHRRG Reviewed; 283 AA.
AC Q5FH34;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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};
GN OrderedLocusNames=ERGA_CDS_04070;
OS Ehrlichia ruminantium (strain Gardel).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Ehrlichia.
OX NCBI_TaxID=302409;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gardel;
RX PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT reveals an active process of genome size plasticity.";
RL J. Bacteriol. 188:2533-2542(2006).
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; CR925677; CAI27859.1; -; Genomic_DNA.
DR RefSeq; WP_011255543.1; NC_006831.1.
DR AlphaFoldDB; Q5FH34; -.
DR SMR; Q5FH34; -.
DR PRIDE; Q5FH34; -.
DR EnsemblBacteria; CAI27859; CAI27859; ERGA_CDS_04070.
DR KEGG; erg:ERGA_CDS_04070; -.
DR HOGENOM; CLU_050669_4_0_5; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR BioCyc; ERUM302409:ERGA_RS02100-MON; -.
DR Proteomes; UP000000533; 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..283
FT /note="ATP synthase gamma chain"
FT /id="PRO_1000053208"
SQ SEQUENCE 283 AA; 32392 MW; 8FB74F273B7BF652 CRC64;
MANLKALFLR MKSVKSIQKT TKVMQMISAA KLRQVQQRLN NARMHMLELS KIIDTNVVSK
NNECTDRHNK KDILLVIMSS DRGLCGNFNN MIVKFAKSYI EELESCGKNV KLLFFGKVAY
NMMCSQYSSK ILDVFSNIQS ITDFLSFKLF LYGSGVDFNQ FIDVMVLFNK FYTTILQKPT
VEQLMPCNID ISVSLKEYYK YEPAYLNVLS TMSLSYILNL MYIAFLENCA SEHSSRVIAM
ESANNNTKEM LSKLVLQYNR SRQAAITTDL IEVISGFESL GNQ
