ATPE_MYCTU
ID ATPE_MYCTU Reviewed; 121 AA.
AC P9WPV1; L0T995; P63662; Q10595;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=ATP synthase epsilon chain;
DE AltName: Full=ATP synthase F1 sector epsilon subunit;
DE AltName: Full=F-ATPase epsilon subunit;
GN Name=atpC; OrderedLocusNames=Rv1311; ORFNames=MTCY373.31;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP PROTEIN SEQUENCE OF 2-18.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2022).
RN [3]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton gradient
CC across the membrane. {ECO:0000250}.
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.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the ATPase epsilon chain family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44068.1; -; Genomic_DNA.
DR PIR; C70775; C70775.
DR RefSeq; NP_215827.1; NC_000962.3.
DR RefSeq; WP_003406708.1; NZ_NVQJ01000030.1.
DR PDB; 2LX5; NMR; -; A=103-120.
DR PDB; 5YIO; NMR; -; A=1-121.
DR PDBsum; 2LX5; -.
DR PDBsum; 5YIO; -.
DR AlphaFoldDB; P9WPV1; -.
DR SMR; P9WPV1; -.
DR STRING; 83332.Rv1311; -.
DR BindingDB; P9WPV1; -.
DR ChEMBL; CHEMBL2364166; -.
DR DrugCentral; P9WPV1; -.
DR PaxDb; P9WPV1; -.
DR DNASU; 886967; -.
DR GeneID; 45425285; -.
DR GeneID; 886967; -.
DR KEGG; mtu:Rv1311; -.
DR TubercuList; Rv1311; -.
DR eggNOG; COG0355; Bacteria.
DR OMA; MGGFAEI; -.
DR PhylomeDB; P9WPV1; -.
DR PRO; PR:P9WPV1; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0045261; C:proton-transporting ATP synthase complex, catalytic core F(1); IBA:GO_Central.
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:0015986; P:proton motive force-driven ATP synthesis; IBA:GO_Central.
DR CDD; cd12152; F1-ATPase_delta; 1.
DR Gene3D; 2.60.15.10; -; 1.
DR HAMAP; MF_00530; ATP_synth_epsil_bac; 1.
DR InterPro; IPR001469; ATP_synth_F1_dsu/esu.
DR InterPro; IPR020546; ATP_synth_F1_dsu/esu_N.
DR InterPro; IPR036771; ATPsynth_dsu/esu_N.
DR PANTHER; PTHR13822; PTHR13822; 1.
DR Pfam; PF02823; ATP-synt_DE_N; 1.
DR SUPFAM; SSF51344; SSF51344; 1.
DR TIGRFAMs; TIGR01216; ATP_synt_epsi; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Cell membrane; CF(1);
KW Direct protein sequencing; Hydrogen ion transport; Ion transport; Membrane;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127"
FT CHAIN 2..121
FT /note="ATP synthase epsilon chain"
FT /id="PRO_0000188166"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:5YIO"
FT STRAND 11..27
FT /evidence="ECO:0007829|PDB:5YIO"
FT STRAND 30..34
FT /evidence="ECO:0007829|PDB:5YIO"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:5YIO"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:5YIO"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:5YIO"
FT STRAND 67..72
FT /evidence="ECO:0007829|PDB:5YIO"
FT TURN 74..76
FT /evidence="ECO:0007829|PDB:5YIO"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:5YIO"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:5YIO"
FT HELIX 92..99
FT /evidence="ECO:0007829|PDB:5YIO"
FT HELIX 104..110
FT /evidence="ECO:0007829|PDB:2LX5"
FT HELIX 112..119
FT /evidence="ECO:0007829|PDB:2LX5"
SQ SEQUENCE 121 AA; 13135 MW; 26E8CC3A5B7BC8D0 CRC64;
MAELNVEIVA VDRNIWSGTA KFLFTRTTVG EIGILPRHIP LVAQLVDDAM VRVEREGEKD
LRIAVDGGFL SVTEEGVSIL AESAEFESEI DEAAAKQDSE SDDPRIAARG RARLRAVGAI
D