ATPG_LIMRD
ID ATPG_LIMRD Reviewed; 314 AA.
AC A5VIR0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Lreu_0466;
OS Limosilactobacillus reuteri (strain DSM 20016) (Lactobacillus reuteri).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Limosilactobacillus.
OX NCBI_TaxID=557436;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20016;
RX PubMed=21379339; DOI=10.1371/journal.pgen.1001314;
RA Frese S.A., Benson A.K., Tannock G.W., Loach D.M., Kim J., Zhang M.,
RA Oh P.L., Heng N.C., Patil P.B., Juge N., Mackenzie D.A., Pearson B.M.,
RA Lapidus A., Dalin E., Tice H., Goltsman E., Land M., Hauser L., Ivanova N.,
RA Kyrpides N.C., Walter J.;
RT "The evolution of host specialization in the vertebrate gut symbiont
RT Lactobacillus reuteri.";
RL PLoS Genet. 7:E1001314-E1001314(2011).
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 membrane {ECO:0000255|HAMAP-Rule:MF_00815};
CC Peripheral membrane protein {ECO:0000255|HAMAP-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; CP000705; ABQ82734.1; -; Genomic_DNA.
DR RefSeq; WP_003666570.1; NZ_AZDD01000022.1.
DR AlphaFoldDB; A5VIR0; -.
DR SMR; A5VIR0; -.
DR STRING; 557436.Lreu_0466; -.
DR PRIDE; A5VIR0; -.
DR EnsemblBacteria; ABQ82734; ABQ82734; Lreu_0466.
DR GeneID; 66470586; -.
DR KEGG; lre:Lreu_0466; -.
DR PATRIC; fig|557436.17.peg.842; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_0_1_9; -.
DR OMA; MQITSAM; -.
DR Proteomes; UP000001991; 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 membrane; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transport.
FT CHAIN 1..314
FT /note="ATP synthase gamma chain"
FT /id="PRO_1000134168"
SQ SEQUENCE 314 AA; 34796 MW; AF5B50EE53E38D9A CRC64;
MPASLAAVKH KIDSTKSTRQ ITSAMQMVST AKLNQIQHHT QTYEVYAEKV KQMLSDLVKS
HSATSAASQD DVYAALFKKR AVKKTGVLVI TSDRGLVGSY NSNIIKQTLD MMAKHNLDKD
NTVFLTVGKT GTEFFKKRGM NVVYEYSGVS DVPTYREVHS IVKTAVQMYS DQVFDEMYMV
YSHYVNRITS NVIVHDVLPI TEKSLLDDEN EAQENTELNN SDVSTAHVSA EYEFEPSDTE
IISALVAQYA ESLIYGAILD AKTSEHSSSA NAMRSATDNA DDIISTLELQ YNRARQAAIT
TEITEITGGM TAQE