ID   ATPG2_PHOPR             Reviewed;         291 AA.
AC   Q6LKZ7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=ATP synthase gamma chain 2 {ECO:0000255|HAMAP-Rule:MF_00815};
DE   AltName: Full=ATP synthase F1 sector gamma subunit 2 {ECO:0000255|HAMAP-Rule:MF_00815};
DE   AltName: Full=F-ATPase gamma subunit 2 {ECO:0000255|HAMAP-Rule:MF_00815};
GN   Name=atpG2 {ECO:0000255|HAMAP-Rule:MF_00815}; OrderedLocusNames=PBPRB0135;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
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; CR378675; CAG22008.1; -; Genomic_DNA.
DR   RefSeq; WP_011220232.1; NC_006371.1.
DR   AlphaFoldDB; Q6LKZ7; -.
DR   SMR; Q6LKZ7; -.
DR   STRING; 298386.PBPRB0135; -.
DR   EnsemblBacteria; CAG22008; CAG22008; PBPRB0135.
DR   KEGG; ppr:PBPRB0135; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_6; -.
DR   OMA; TRAMYLI; -.
DR   OrthoDB; 1701531at2; -.
DR   Proteomes; UP000000593; Chromosome 2.
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   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   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..291
FT                   /note="ATP synthase gamma chain 2"
FT                   /id="PRO_0000073338"
FT   REGION          187..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   291 AA;  32639 MW;  A212396DD7A033D8 CRC64;
     MANAKEIRTK IASVQNTQKI TSAMEMVAAS KMRKVQDNMA ATRPYAENMR KVISHVASGS
     LEYKHPYLEE REAKRVAYII ISSDRGLCGG LNSNLFKRAL TDMRQWQEKN VEVDLTLIGS
     KAISFFHRFG NVIAQTSGLG DKPKLEDLLG AVTAMLEHFD DGKIDRLYLV YNEFVNTMVQ
     NPRITQLLPH PDKDESQDSK PNDATSRWDY IYEPDPKDIL NALMLRYIES QVYQGTVESI
     ACEQAARMVA MKSATDNAGD IINDLQLVYN KARQSAITQE LSEIVAGAQA V