ATPG_MALP2
ID ATPG_MALP2 Reviewed; 286 AA.
AC Q8EWY9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=MYPE610;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC43851.1; -; Genomic_DNA.
DR RefSeq; WP_011076887.1; NC_004432.1.
DR AlphaFoldDB; Q8EWY9; -.
DR SMR; Q8EWY9; -.
DR STRING; 272633.26453519; -.
DR EnsemblBacteria; BAC43851; BAC43851; BAC43851.
DR KEGG; mpe:MYPE610; -.
DR eggNOG; COG0224; Bacteria.
DR HOGENOM; CLU_050669_4_1_14; -.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR Proteomes; UP000002522; 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..286
FT /note="ATP synthase gamma chain"
FT /id="PRO_0000073323"
SQ SEQUENCE 286 AA; 32516 MW; 4F61E2EB43146F53 CRC64;
MASLNEIKKR IKIIESTSKI TNAMKLVSSA KLKKQKELFL NESIYYKKFY DLFTYIKSNS
DSEILSLKKS EEGKTIWLAF FSSMGLCGSF NLNIVKELQK HIKSNDEIWL IGKKGKNLIK
SKGIEAEISL DLELDDKDIN FDLFHIIAEN LLAKYKNDYN IKSIKVIYSK FVNSLSFTPS
VFSLLPLDKA IEKPRLDKPN NGADFSIQPN ANDVFESILI DYLATCIHGA IVESKVCENA
SRRNAMDSAT KNANELIKNY KLEFNRKRQS EITQEITEIV SGAKGE
