ATPG_MYCS2
ID ATPG_MYCS2 Reviewed; 307 AA.
AC A0R201; I7FIQ7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
GN OrderedLocusNames=MSMEG_4937, MSMEI_4810;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK75438.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP41255.1; -; Genomic_DNA.
DR RefSeq; WP_003896329.1; NZ_SIJM01000067.1.
DR RefSeq; YP_889189.1; NC_008596.1.
DR PDB; 6FOC; X-ray; 4.00 A; G=1-307.
DR PDB; 7JG5; EM; 3.40 A; G=1-307.
DR PDB; 7JG6; EM; 3.70 A; G=1-307.
DR PDB; 7JG7; EM; 3.50 A; G=1-307.
DR PDB; 7JG8; EM; 3.30 A; G=1-307.
DR PDB; 7JG9; EM; 3.40 A; G=1-307.
DR PDB; 7JGA; EM; 3.20 A; G=1-307.
DR PDB; 7NJK; EM; 2.52 A; G=1-307.
DR PDB; 7NJL; EM; 2.71 A; G=1-307.
DR PDB; 7NJM; EM; 2.84 A; G=1-307.
DR PDB; 7NJN; EM; 2.64 A; G=1-307.
DR PDB; 7NJO; EM; 2.92 A; G=1-307.
DR PDB; 7NJP; EM; 2.84 A; G=1-307.
DR PDB; 7NJQ; EM; 2.67 A; G=1-307.
DR PDB; 7NJR; EM; 2.56 A; G=1-307.
DR PDB; 7NJS; EM; 2.46 A; G=1-307.
DR PDB; 7NK7; EM; 2.11 A; G=1-307.
DR PDB; 7NK9; EM; 2.90 A; G=1-307.
DR PDB; 7NKB; EM; 2.90 A; G=1-307.
DR PDB; 7NKH; EM; 2.78 A; G=1-307.
DR PDB; 7NKJ; EM; 2.17 A; G=1-307.
DR PDB; 7NKK; EM; 3.60 A; G=1-307.
DR PDB; 7NKN; EM; 2.71 A; G=1-307.
DR PDB; 7NKP; EM; 4.06 A; G=1-307.
DR PDB; 7NL9; EM; 2.86 A; G=1-307.
DR PDBsum; 6FOC; -.
DR PDBsum; 7JG5; -.
DR PDBsum; 7JG6; -.
DR PDBsum; 7JG7; -.
DR PDBsum; 7JG8; -.
DR PDBsum; 7JG9; -.
DR PDBsum; 7JGA; -.
DR PDBsum; 7NJK; -.
DR PDBsum; 7NJL; -.
DR PDBsum; 7NJM; -.
DR PDBsum; 7NJN; -.
DR PDBsum; 7NJO; -.
DR PDBsum; 7NJP; -.
DR PDBsum; 7NJQ; -.
DR PDBsum; 7NJR; -.
DR PDBsum; 7NJS; -.
DR PDBsum; 7NK7; -.
DR PDBsum; 7NK9; -.
DR PDBsum; 7NKB; -.
DR PDBsum; 7NKH; -.
DR PDBsum; 7NKJ; -.
DR PDBsum; 7NKK; -.
DR PDBsum; 7NKN; -.
DR PDBsum; 7NKP; -.
DR PDBsum; 7NL9; -.
DR AlphaFoldDB; A0R201; -.
DR SMR; A0R201; -.
DR STRING; 246196.MSMEI_4810; -.
DR PRIDE; A0R201; -.
DR EnsemblBacteria; ABK75438; ABK75438; MSMEG_4937.
DR EnsemblBacteria; AFP41255; AFP41255; MSMEI_4810.
DR GeneID; 66736259; -.
DR KEGG; msg:MSMEI_4810; -.
DR KEGG; msm:MSMEG_4937; -.
DR PATRIC; fig|246196.19.peg.4816; -.
DR eggNOG; COG0224; Bacteria.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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 InterPro; IPR023632; ATP_synth_F1_gsu_CS.
DR PANTHER; PTHR11693; PTHR11693; 2.
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 3D-structure; ATP synthesis; Cell membrane; CF(1); Hydrogen ion transport;
KW Ion transport; Membrane; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:18955433"
FT CHAIN 2..307
FT /note="ATP synthase gamma chain"
FT /id="PRO_1000053257"
FT HELIX 4..59
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 76..82
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 85..87
FT /evidence="ECO:0007829|PDB:7NJN"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 92..109
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 121..130
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 134..138
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 147..163
FT /evidence="ECO:0007829|PDB:7NJS"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:7NJR"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 183..190
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:7NJR"
FT STRAND 196..210
FT /evidence="ECO:0007829|PDB:7NJS"
FT STRAND 223..226
FT /evidence="ECO:0007829|PDB:7NJS"
FT HELIX 228..303
FT /evidence="ECO:0007829|PDB:7NJS"
SQ SEQUENCE 307 AA; 33398 MW; 2EB6BAD215F65F61 CRC64;
MAATLRELRG RIRSAGSIKK ITKAQELIAT SRIAKAQARV EAARPYAAEI TNMLTELAGA
SALDHPLLVE RKQPKRAGVL VVSSDRGLCG AYNANVLRRA EELFSLLRDE GKDPVLYVVG
RKALGYFSFR QRTVVESWTG FSERPTYENA REIADTLVNA FMAGADDEGD DAGADGILGV
DELHIVFTEF RSMLSQTAVA RRAAPMEVEY VGEVETGPRT LYSFEPDPET LFDALLPRYI
ATRVYAALLE AAASESASRR RAMKSATDNA DDLIKALTLA ANRERQAQIT QEISEIVGGA
NALAGSK
