ATPG_PROMO
ID ATPG_PROMO Reviewed; 282 AA.
AC P29710;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=ATP synthase gamma chain, sodium ion specific;
DE AltName: Full=F-ATPase gamma subunit, sodium ion specific;
GN Name=atpG; Synonyms=uncG;
OS Propionigenium modestum.
OC Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Propionigenium.
OX NCBI_TaxID=2333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 2376 / Gra Succ2;
RX PubMed=1533602; DOI=10.1016/0378-1097(92)90559-7;
RA Krumholz L.R., Esser U., Simoni R.D.;
RT "Characterization of the genes coding for the F1F0 subunits of the sodium
RT dependent ATPase of Propionigenium modestum.";
RL FEMS Microbiol. Lett. 70:37-41(1992).
RN [2]
RP PROTEIN SEQUENCE OF 2-8.
RX PubMed=8422943; DOI=10.1016/0014-5793(93)81742-i;
RA Gerike U., Dimroth P.;
RT "N-terminal amino acid sequences of the subunits of the Na(+)-translocating
RT F1F0 ATPase from Propionigenium modestum.";
RL FEBS Lett. 316:89-92(1993).
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.
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.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- MISCELLANEOUS: The ATPase of P.modestum is of special interest because
CC it uses sodium ions instead of protons as the physiological coupling
CC ion.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
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DR EMBL; X58461; CAA41373.1; -; Genomic_DNA.
DR PIR; S29040; S29040.
DR AlphaFoldDB; P29710; -.
DR SMR; P29710; -.
DR TCDB; 3.A.2.1.2; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
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 GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Sodium; Sodium transport; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8422943"
FT CHAIN 2..282
FT /note="ATP synthase gamma chain, sodium ion specific"
FT /id="PRO_0000073344"
SQ SEQUENCE 282 AA; 31813 MW; F3408B38237B4F31 CRC64;
MAAGKEIKSR ISSVQSTRQI TKAMEIVSST KFKKFQALVN QSKPYSGSMD KVLANLAAGI
KNERHPLFDG KTEVKRIGII VMTSDRGLCG GFNSSTLKEM EKLIVANPDK EVSVIAIGKK
GRDYCKKKDR DLKAEYIQLI PETMFDKAKE ISENIVEYFY EDIFDEVYLI YNEFISALST
ELIVKKLLPI ERIEVQDNTT YIFEPSVEDI LSSLLPKYLN IQLYQAILEN TASEHSARKN
AMKNATDNAE DMIKDLTLQY NRERQAAITQ EISEIVSGAS AL