ATPL_THEVB
ID ATPL_THEVB Reviewed; 82 AA.
AC Q8DLP7;
DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=ATP synthase subunit c;
DE AltName: Full=ATP synthase F(0) sector subunit c;
DE AltName: Full=F-type ATPase subunit c;
DE Short=F-ATPase subunit c;
DE AltName: Full=Lipid-binding protein;
GN Name=atpE; Synonyms=atpH; OrderedLocusNames=tlr0431;
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: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation (By similarity).
CC {ECO:0000250}.
CC -!- FUNCTION: Key component of the F(0) channel; it plays a direct role in
CC translocation across the membrane. A homomeric c-ring of between 10-14
CC subunits forms the central stalk rotor element with the F(1) delta and
CC epsilon subunits (By similarity). {ECO:0000250}.
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 -!- ACTIVITY REGULATION: Inhibited by dicyclohexylcarbodiimide.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has four main
CC subunits: a(1), b(1), b'(1) and c(10-14). The alpha and beta chains
CC form an alternating ring which encloses part of the gamma chain. F(1)
CC is attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta, b and b'
CC chains. {ECO:0000269|PubMed:18206981}.
CC -!- SUBCELLULAR LOCATION: Cellular thylakoid membrane
CC {ECO:0000269|PubMed:18206981}; Multi-pass membrane protein
CC {ECO:0000250}.
CC -!- MASS SPECTROMETRY: Mass=8238.17; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:18206981};
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC07983.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000039; BAC07983.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_681221.1; NC_004113.1.
DR RefSeq; WP_024125083.1; NC_004113.1.
DR AlphaFoldDB; Q8DLP7; -.
DR SMR; Q8DLP7; -.
DR STRING; 197221.22294152; -.
DR EnsemblBacteria; BAC07983; BAC07983; BAC07983.
DR KEGG; tel:tlr0431; -.
DR PATRIC; fig|197221.4.peg.455; -.
DR eggNOG; COG0636; Bacteria.
DR OMA; NIATVGY; -.
DR OrthoDB; 2078221at2; -.
DR Proteomes; UP000000440; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031676; C:plasma membrane-derived thylakoid membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.20.10; -; 1.
DR HAMAP; MF_01396; ATP_synth_c_bact; 1.
DR InterPro; IPR005953; ATP_synth_csu_bac/chlpt.
DR InterPro; IPR000454; ATP_synth_F0_csu.
DR InterPro; IPR020537; ATP_synth_F0_csu_DDCD_BS.
DR InterPro; IPR038662; ATP_synth_F0_csu_sf.
DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom.
DR InterPro; IPR035921; F/V-ATP_Csub_sf.
DR PANTHER; PTHR10031; PTHR10031; 1.
DR Pfam; PF00137; ATP-synt_C; 1.
DR PRINTS; PR00124; ATPASEC.
DR SUPFAM; SSF81333; SSF81333; 1.
DR TIGRFAMs; TIGR01260; ATP_synt_c; 1.
DR PROSITE; PS00605; ATPASE_C; 1.
PE 1: Evidence at protein level;
KW ATP synthesis; CF(0); Hydrogen ion transport; Ion transport; Lipid-binding;
KW Membrane; Reference proteome; Thylakoid; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..82
FT /note="ATP synthase subunit c"
FT /id="PRO_0000365934"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 61
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000250"
SQ SEQUENCE 82 AA; 8207 MW; 32739CF45661DA06 CRC64;
MNPLIASASV LAAALAIGLA SLGPGLAQGN ASGQALEGIA RQPEAEGKIR GTLLLSLAFM
ESLTIYGLVI ALVLLFANPF AS
