ATPL_MYCLE
ID ATPL_MYCLE Reviewed; 81 AA.
AC P45828;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 135.
DE RecName: Full=ATP synthase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=ATP synthase F(0) sector subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=F-type ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE Short=F-ATPase subunit c {ECO:0000255|HAMAP-Rule:MF_01396};
DE AltName: Full=Lipid-binding protein {ECO:0000255|HAMAP-Rule:MF_01396};
GN Name=atpE {ECO:0000255|HAMAP-Rule:MF_01396}; OrderedLocusNames=ML1140;
OS Mycobacterium leprae (strain TN).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=272631;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Smith D.R., Robison K.;
RL Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TN;
RX PubMed=11234002; DOI=10.1038/35059006;
RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA Barrell B.G.;
RT "Massive gene decay in the leprosy bacillus.";
RL Nature 409:1007-1011(2001).
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. {ECO:0000255|HAMAP-
CC Rule:MF_01396}.
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. {ECO:0000255|HAMAP-Rule:MF_01396}.
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 three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC 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 and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01396}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01396};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01396}.
CC -!- MISCELLANEOUS: Dicyclohexylcarbodiimide (DCDD) binding to the active
CC glutamate residue inhibits ATPase in vitro. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ATPase C chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01396}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U15186; AAA63107.1; -; Genomic_DNA.
DR EMBL; AL583920; CAC31521.1; -; Genomic_DNA.
DR PIR; T09979; T09979.
DR RefSeq; NP_301834.1; NC_002677.1.
DR RefSeq; WP_010908158.1; NC_002677.1.
DR AlphaFoldDB; P45828; -.
DR SMR; P45828; -.
DR STRING; 272631.ML1140; -.
DR EnsemblBacteria; CAC31521; CAC31521; CAC31521.
DR KEGG; mle:ML1140; -.
DR PATRIC; fig|272631.5.peg.2062; -.
DR Leproma; ML1140; -.
DR eggNOG; COG0636; Bacteria.
DR HOGENOM; CLU_148047_1_2_11; -.
DR OMA; QPELMNE; -.
DR Proteomes; UP000000806; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma 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 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 3: Inferred from homology;
KW ATP synthesis; Cell membrane; CF(0); Hydrogen ion transport; Ion transport;
KW Lipid-binding; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..81
FT /note="ATP synthase subunit c"
FT /id="PRO_0000112153"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
FT SITE 61
FT /note="Reversibly protonated during proton transport"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01396"
SQ SEQUENCE 81 AA; 8205 MW; E5456207EE9E0C13 CRC64;
MDPMIAQGAL IGGGLIMAGG AIGAGIGDGM AGNALVSGIA RQPEAQSRLF TPFFITVGLV
EAAYFINLAF MALFVFATPV K
