ATPG_BACSU
ID ATPG_BACSU Reviewed; 287 AA.
AC P37810; O32279;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
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=BSU36820;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7961438; DOI=10.1128/jb.176.22.6802-6811.1994;
RA Santana M., Ionescu M.S., Vertes A., Longin R., Kunst F., Danchin A.,
RA Glaser P.;
RT "Bacillus subtilis F0F1 ATPase: DNA sequence of the atp operon and
RT characterization of atp mutants.";
RL J. Bacteriol. 176:6802-6811(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH SPOIIIJ AND YQJG.
RC STRAIN=168;
RX PubMed=19717609; DOI=10.1128/jb.00853-09;
RA Saller M.J., Fusetti F., Driessen A.J.;
RT "Bacillus subtilis SpoIIIJ and YqjG function in membrane protein
RT biogenesis.";
RL J. Bacteriol. 191:6749-6757(2009).
RN [4]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
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 (Probable). The F(1)F(0) complex interacts with
CC SpoIIIJ and YqjG; YqgA is found in the same complex (By similarity)
CC (PubMed:19717609). Interacts with FloT (PubMed:23651456).
CC {ECO:0000255|HAMAP-Rule:MF_00815, ECO:0000269|PubMed:19717609,
CC ECO:0000269|PubMed:23651456, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00815,
CC ECO:0000269|PubMed:23651456}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00815}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Peripheral membrane protein.
CC Note=Present in detergent-resistant membrane (DRM) fractions that may
CC be equivalent to eukaryotic membrane rafts; these rafts include
CC proteins involved in signaling, molecule trafficking and protein
CC secretion. {ECO:0000269|PubMed:23651456}.
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00815}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA82259.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; Z28592; CAA82259.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15699.1; -; Genomic_DNA.
DR PIR; C69592; C69592.
DR RefSeq; NP_391563.1; NC_000964.3.
DR RefSeq; WP_003244388.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P37810; -.
DR SMR; P37810; -.
DR IntAct; P37810; 2.
DR STRING; 224308.BSU36820; -.
DR jPOST; P37810; -.
DR PaxDb; P37810; -.
DR PRIDE; P37810; -.
DR EnsemblBacteria; CAB15699; CAB15699; BSU_36820.
DR GeneID; 936989; -.
DR KEGG; bsu:BSU36820; -.
DR PATRIC; fig|224308.179.peg.3988; -.
DR eggNOG; COG0224; Bacteria.
DR InParanoid; P37810; -.
DR OMA; MQITSAM; -.
DR PhylomeDB; P37810; -.
DR BioCyc; BSUB:BSU36820-MON; -.
DR SABIO-RK; P37810; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
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 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 membrane; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Transport.
FT CHAIN 1..287
FT /note="ATP synthase gamma chain"
FT /id="PRO_0000073234"
SQ SEQUENCE 287 AA; 31655 MW; 3A135C503FD70862 CRC64;
MASLRDIKSR ITSTKKTSQI TKAMQMVSAA KLNRAENNAK SFVPYMDKIQ EVVSNVGRVS
GNVKHPMLLS REVKKTAYLV ITSDRGLAGA FNSSVLRSAY QAMQERHQSK DEYAVIAIGR
VGRDFFKKRE IPIISELTGL GDEVTFTEIK DLARQTIQMF IDGAFDELHL VYNHFVSAIT
QEVTEKKLLP LSDLGSGGGK RTASYEFEPS EEEVLEVLLP QYAESLIFGA LLDSKASEHA
ARMTAMKNAT DNAKELIDSL SLSYNRARQA AITQEITEIV GGAAALE
