ATPG_THEVB
ID ATPG_THEVB Reviewed; 315 AA.
AC Q8DLU1;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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 Synonyms=atpC {ECO:0000255|HAMAP-Rule:MF_00815}; OrderedLocusNames=tll0385;
OS Thermosynechococcus vestitus (strain NIES-2133 / IAM M-273 / BP-1).
OC Bacteria; Cyanobacteria; Pseudanabaenales; Thermosynechococcaceae;
OC Thermosynechococcus.
OX NCBI_TaxID=197221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=12240834; DOI=10.1093/dnares/9.4.123;
RA Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S.,
RA Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C.,
RA Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takeuchi C., Yamada M., Tabata S.;
RT "Complete genome structure of the thermophilic cyanobacterium
RT Thermosynechococcus elongatus BP-1.";
RL DNA Res. 9:123-130(2002).
RN [2]
RP FUNCTION, MASS SPECTROMETRY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=NIES-2133 / IAM M-273 / BP-1;
RX PubMed=18206981; DOI=10.1016/j.bbamem.2007.12.017;
RA Suhai T., Dencher N.A., Poetsch A., Seelert H.;
RT "Remarkable stability of the proton translocating F1FO-ATP synthase from
RT the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1.";
RL Biochim. Biophys. Acta 1778:1131-1140(2008).
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 -!- FUNCTION: The complex from the organism is particularly stable to
CC disruption and remains functional after 6 hrs at 55 degrees Celsius.
CC {ECO:0000269|PubMed:18206981}.
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 four main
CC subunits: a(1), b(1), b'(1) and c(9-12). {ECO:0000269|PubMed:18206981}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-
CC Rule:MF_00815, ECO:0000269|PubMed:18206981}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_00815, ECO:0000269|PubMed:18206981}.
CC -!- MASS SPECTROMETRY: Mass=35013; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18206981};
CC -!- SIMILARITY: Belongs to the ATPase gamma chain family.
CC {ECO:0000255|HAMAP-Rule:MF_00815}.
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DR EMBL; BA000039; BAC07937.1; -; Genomic_DNA.
DR RefSeq; NP_681175.1; NC_004113.1.
DR RefSeq; WP_011056240.1; NC_004113.1.
DR PDB; 5ZWL; X-ray; 1.98 A; G=12-285.
DR PDBsum; 5ZWL; -.
DR AlphaFoldDB; Q8DLU1; -.
DR SMR; Q8DLU1; -.
DR STRING; 197221.22294106; -.
DR EnsemblBacteria; BAC07937; BAC07937; BAC07937.
DR KEGG; tel:tll0385; -.
DR PATRIC; fig|197221.4.peg.407; -.
DR eggNOG; COG0224; Bacteria.
DR OMA; MQITSAM; -.
DR OrthoDB; 1701531at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid 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 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 3D-structure; ATP synthesis; CF(1); Hydrogen ion transport; Ion transport;
KW Membrane; Reference proteome; Thylakoid; Transport.
FT CHAIN 1..315
FT /note="ATP synthase gamma chain"
FT /id="PRO_0000073402"
FT HELIX 28..41
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 93..110
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 148..163
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 183..192
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 204..210
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:5ZWL"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5ZWL"
FT HELIX 239..276
FT /evidence="ECO:0007829|PDB:5ZWL"
SQ SEQUENCE 315 AA; 34963 MW; 700E29F8587195D1 CRC64;
MANLKAIRDR IKTIKDTRKI TEAMRLVAAA KVRRAQEQVM ASRPFADRLA QVLYSLQTRL
RFEDVDLPLL AKRPVKTVAL LVVTGDRGLC GGYNTNVIRR AKERLQELEA EGLKYTLVIV
GRKAAQYFQR RDYPIDAVYS GLEQIPSASE AGQIASELLS LFLSETVDRV ELIYTKFVSL
ISSKPVVQTL LPLDPQGLET ADDEIFRLTT RGSHLEVNRE KVTSTLPALP SDMIFEQDPL
QILDALLPLY LNNQLLRALQ EAAASELAAR MTAMNNASDN AQALIGTLTL SYNKARQAAI
TQEILEVVAG AEALR
