ID   ATPG_ECOLI              Reviewed;         287 AA.
AC   P0ABA6; P00837; P00838; Q2M851;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=ATP synthase gamma chain;
DE   AltName: Full=ATP synthase F1 sector gamma subunit;
DE   AltName: Full=F-ATPase gamma subunit;
GN   Name=atpG; Synonyms=papC, uncG; OrderedLocusNames=b3733, JW3711;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6395859; DOI=10.1042/bj2240799;
RA   Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT   "DNA sequence around the Escherichia coli unc operon. Completion of the
RT   sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT   phoS.";
RL   Biochem. J. 224:799-815(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6272217; DOI=10.1093/nar/9.20.5287;
RA   Saraste M., Gay N.J., Eberle A., Runswick M.J., Walker J.E.;
RT   "The atp operon: nucleotide sequence of the genes for the gamma, beta, and
RT   epsilon subunits of Escherichia coli ATP synthase.";
RL   Nucleic Acids Res. 9:5287-5296(1981).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6277310; DOI=10.1016/0006-291x(81)90494-0;
RA   Kanazawa H., Kayano T., Mabuchi K., Futai M.;
RT   "Nucleotide sequence of the genes coding for alpha, beta and gamma subunits
RT   of the proton-translocating ATPase of Escherichia coli.";
RL   Biochem. Biophys. Res. Commun. 103:604-612(1981).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6301339; DOI=10.1111/j.1749-6632.1982.tb25731.x;
RA   Kanazawa H., Futai M.;
RT   "Structure and function of H+-ATPase: what we have learned from Escherichia
RT   coli H+-ATPase.";
RL   Ann. N. Y. Acad. Sci. 402:45-64(1982).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT   organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [8]
RP   PROTEIN SEQUENCE OF 2-9; 72-81; 203-208 AND 214-220.
RX   PubMed=7508444; DOI=10.1016/s0021-9258(17)41802-3;
RA   Tang C., Wilkens S., Capaldi R.A.;
RT   "Structure of the gamma subunit of Escherichia coli F1 ATPase probed in
RT   trypsin digestion and biotin-avidin binding studies.";
RL   J. Biol. Chem. 269:4467-4472(1994).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 261-287.
RX   PubMed=2138624; DOI=10.1016/s0021-9258(19)34081-5;
RA   Iwamoto A., Miki J., Maeda M., Futai M.;
RT   "H(+)-ATPase gamma subunit of Escherichia coli. Role of the conserved
RT   carboxyl-terminal region.";
RL   J. Biol. Chem. 265:5043-5048(1990).
RN   [10]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=BL21-DE3;
RX   PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA   Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA   von Heijne G., Daley D.O.;
RT   "Protein complexes of the Escherichia coli cell envelope.";
RL   J. Biol. Chem. 280:34409-34419(2005).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (4.4 ANGSTROMS).
RX   PubMed=10570135; DOI=10.1073/pnas.96.24.13697;
RA   Hausrath A.C., Grueber G., Matthews B.W., Capaldi R.A.;
RT   "Structural features of the gamma subunit of the Escherichia coli F(1)
RT   ATPase revealed by a 4.4-A resolution map obtained by X-ray
RT   crystallography.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:13697-13702(1999).
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. {ECO:0000269|PubMed:16079137}.
CC   -!- INTERACTION:
CC       P0ABA6; P0A6E6: atpC; NbExp=5; IntAct=EBI-544306, EBI-544362;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000269|PubMed:16079137}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:16079137}.
CC   -!- SIMILARITY: Belongs to the ATPase gamma chain family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA23597.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA23597.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR   EMBL; X01631; CAA25781.1; -; Genomic_DNA.
DR   EMBL; V00267; CAA23526.1; -; Genomic_DNA.
DR   EMBL; J01594; AAA24736.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; V00312; CAA23597.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; M25464; AAA83874.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62085.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76756.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77555.1; -; Genomic_DNA.
DR   EMBL; M34095; AAA24742.1; -; Genomic_DNA.
DR   PIR; A01038; PWECG.
DR   RefSeq; NP_418189.1; NC_000913.3.
DR   RefSeq; WP_000896498.1; NZ_STEB01000015.1.
DR   PDB; 1D8S; X-ray; 4.40 A; G=1-287.
DR   PDB; 1FS0; X-ray; 2.10 A; G=19-248.
DR   PDB; 3OAA; X-ray; 3.26 A; G/O/W/e=2-287.
DR   PDB; 5T4O; EM; 6.90 A; G=1-287.
DR   PDB; 5T4P; EM; 7.77 A; G=1-287.
DR   PDB; 5T4Q; EM; 8.53 A; G=1-287.
DR   PDB; 6OQR; EM; 3.10 A; G=1-287.
DR   PDB; 6OQS; EM; 3.30 A; G=1-287.
DR   PDB; 6OQT; EM; 3.10 A; G=1-287.
DR   PDB; 6OQU; EM; 3.20 A; G=1-287.
DR   PDB; 6OQV; EM; 3.30 A; G=1-287.
DR   PDB; 6OQW; EM; 3.10 A; G=1-287.
DR   PDB; 6PQV; EM; 3.30 A; G=1-287.
DR   PDB; 6WNQ; EM; 3.40 A; G=1-287.
DR   PDB; 6WNR; EM; 3.30 A; G=1-287.
DR   PDBsum; 1D8S; -.
DR   PDBsum; 1FS0; -.
DR   PDBsum; 3OAA; -.
DR   PDBsum; 5T4O; -.
DR   PDBsum; 5T4P; -.
DR   PDBsum; 5T4Q; -.
DR   PDBsum; 6OQR; -.
DR   PDBsum; 6OQS; -.
DR   PDBsum; 6OQT; -.
DR   PDBsum; 6OQU; -.
DR   PDBsum; 6OQV; -.
DR   PDBsum; 6OQW; -.
DR   PDBsum; 6PQV; -.
DR   PDBsum; 6WNQ; -.
DR   PDBsum; 6WNR; -.
DR   AlphaFoldDB; P0ABA6; -.
DR   EMDB; EMD-20167; -.
DR   EMDB; EMD-20168; -.
DR   EMDB; EMD-20169; -.
DR   EMDB; EMD-20170; -.
DR   EMDB; EMD-20171; -.
DR   EMDB; EMD-20172; -.
DR   EMDB; EMD-20454; -.
DR   EMDB; EMD-21854; -.
DR   EMDB; EMD-21855; -.
DR   EMDB; EMD-8357; -.
DR   EMDB; EMD-8358; -.
DR   EMDB; EMD-8359; -.
DR   SMR; P0ABA6; -.
DR   BioGRID; 852545; 6.
DR   ComplexPortal; CPX-4022; ATP synthase complex.
DR   DIP; DIP-35938N; -.
DR   IntAct; P0ABA6; 15.
DR   STRING; 511145.b3733; -.
DR   TCDB; 3.A.2.1.1; the h+- or na+-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR   jPOST; P0ABA6; -.
DR   PaxDb; 511145-b3733; -.
DR   EnsemblBacteria; AAC76756; AAC76756; b3733.
DR   GeneID; 83578727; -.
DR   GeneID; 948243; -.
DR   KEGG; ecj:JW3711; -.
DR   KEGG; eco:b3733; -.
DR   PATRIC; fig|1411691.4.peg.2967; -.
DR   EchoBASE; EB0102; -.
DR   eggNOG; COG0224; Bacteria.
DR   HOGENOM; CLU_050669_0_1_6; -.
DR   InParanoid; P0ABA6; -.
DR   OMA; MQITSAM; -.
DR   OrthoDB; 9812769at2; -.
DR   PhylomeDB; P0ABA6; -.
DR   BioCyc; EcoCyc:ATPG-MONOMER; -.
DR   BioCyc; MetaCyc:ATPG-MONOMER; -.
DR   BRENDA; 7.1.2.2; 2026.
DR   EvolutionaryTrace; P0ABA6; -.
DR   PRO; PR:P0ABA6; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; NAS:ComplexPortal.
DR   GO; GO:0045259; C:proton-transporting ATP synthase complex; IPI:ComplexPortal.
DR   GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IMP:EcoliWiki.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IDA:EcoCyc.
DR   GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IDA:EcoCyc.
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; IMP:ComplexPortal.
DR   CDD; cd12151; F1-ATPase_gamma; 1.
DR   Gene3D; 3.40.1380.10; -; 1.
DR   Gene3D; 1.10.287.80; ATP synthase, gamma subunit, helix hairpin domain; 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   NCBIfam; TIGR01146; ATPsyn_F1gamma; 1.
DR   PANTHER; PTHR11693; ATP SYNTHASE GAMMA CHAIN; 1.
DR   PANTHER; PTHR11693:SF41; ATP SYNTHASE GAMMA CHAIN 1, CHLOROPLASTIC; 1.
DR   Pfam; PF00231; ATP-synt; 1.
DR   PRINTS; PR00126; ATPASEGAMMA.
DR   SUPFAM; SSF52943; ATP synthase (F1-ATPase), gamma subunit; 1.
DR   PROSITE; PS00153; ATPASE_GAMMA; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(1);
KW   Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW   Reference proteome; Transport.
FT   CHAIN           1..287
FT                   /note="ATP synthase gamma chain"
FT                   /id="PRO_0000073282"
FT   HELIX           20..57
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   HELIX           66..68
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   STRAND          84..86
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   HELIX           91..108
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   STRAND          112..119
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   HELIX           120..129
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   STRAND          133..137
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   HELIX           147..161
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   TURN            162..164
FT                   /evidence="ECO:0007829|PDB:6OQT"
FT   STRAND          168..177
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   STRAND          180..190
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   HELIX           198..203
FT                   /evidence="ECO:0007829|PDB:6OQR"
FT   STRAND          207..210
FT                   /evidence="ECO:0007829|PDB:1FS0"
FT   HELIX           212..247
FT                   /evidence="ECO:0007829|PDB:1FS0"
SQ   SEQUENCE   287 AA;  31577 MW;  2417A4B8FBDB8EF8 CRC64;
     MAGAKEIRSK IASVQNTQKI TKAMEMVAAS KMRKSQDRMA ASRPYAETMR KVIGHLAHGN
     LEYKHPYLED RDVKRVGYLV VSTDRGLCGG LNINLFKKLL AEMKTWTDKG VQCDLAMIGS
     KGVSFFNSVG GNVVAQVTGM GDNPSLSELI GPVKVMLQAY DEGRLDKLYI VSNKFINTMS
     QVPTISQLLP LPASDDDDLK HKSWDYLYEP DPKALLDTLL RRYVESQVYQ GVVENLASEQ
     AARMVAMKAA TDNGGSLIKE LQLVYNKARQ ASITQELTEI VSGAAAV
//