ID   ECCA1_MYCLE             Reviewed;         573 AA.
AC   O33089;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=ESX-1 secretion system protein EccA1 {ECO:0000305};
DE   AltName: Full=ESX conserved component A1 {ECO:0000303|PubMed:19876390};
DE   AltName: Full=Type VII secretion system protein EccA1 {ECO:0000305};
DE            Short=T7SS protein EccA1 {ECO:0000305};
GN   Name=eccA1 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=ML0055;
GN   ORFNames=MLCB628.18c;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
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).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=19876390; DOI=10.1371/journal.ppat.1000507;
RA   Bitter W., Houben E.N., Bottai D., Brodin P., Brown E.J., Cox J.S.,
RA   Derbyshire K., Fortune S.M., Gao L.Y., Liu J., Gey van Pittius N.C.,
RA   Pym A.S., Rubin E.J., Sherman D.R., Cole S.T., Brosch R.;
RT   "Systematic genetic nomenclature for type VII secretion systems.";
RL   PLoS Pathog. 5:E1000507-E1000507(2009).
CC   -!- FUNCTION: Part of the ESX-1 / type VII specialized secretion system
CC       (T7SS), which exports several proteins including EsxA and EsxB. EccA1
CC       exhibits ATPase activity and may provide energy for the export of ESX-1
CC       substrates (By similarity). {ECO:0000250|UniProtKB:P9WPH9}.
CC   -!- SUBUNIT: Part of the ESX-1 / type VII secretion system (T7SS), which is
CC       composed of cytosolic and membrane components (By similarity).
CC       {ECO:0000250|UniProtKB:P9WPH9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2HSU9}.
CC   -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR   EMBL; Y14967; CAA75205.1; -; Genomic_DNA.
DR   EMBL; AL583917; CAC29563.1; -; Genomic_DNA.
DR   PIR; T10037; T10037.
DR   RefSeq; NP_301168.1; NC_002677.1.
DR   RefSeq; WP_010907493.1; NC_002677.1.
DR   AlphaFoldDB; O33089; -.
DR   SMR; O33089; -.
DR   STRING; 272631.ML0055; -.
DR   EnsemblBacteria; CAC29563; CAC29563; CAC29563.
DR   KEGG; mle:ML0055; -.
DR   PATRIC; fig|272631.5.peg.78; -.
DR   Leproma; ML0055; -.
DR   eggNOG; COG0464; Bacteria.
DR   HOGENOM; CLU_008749_5_0_11; -.
DR   OMA; VEAGEQN; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041627; AAA_lid_6.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR000641; CbxX/CfxQ.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR023835; T7SS_EccA.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17866; AAA_lid_6; 1.
DR   PRINTS; PR00819; CBXCFQXSUPER.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03922; T7SS_EccA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..573
FT                   /note="ESX-1 secretion system protein EccA1"
FT                   /id="PRO_0000063048"
FT   BINDING         334..341
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   573 AA;  62342 MW;  A60CD0F7D73DD098 CRC64;
     MIDRLGSLFE SAASMLPMSE ARSFELFTEI TNYDETACDA WIGRIRCGDT DRVTLFRAWY
     SRRNFGQLSG SVQIPMTTLN ARVPIGGLYG DITYPVTSPL AITMGFAACE AAQGNFADAM
     EAIDATSITG SEHLVAWLKA VVYGAAERWT DVIDEVKGAG KWPDKFLAGA AGVAHGVAAA
     NLGLFTEAER RLTEANDSPA GEACARSIAW YLAMARRSQG NEDAAVALLE WLQTTHPESK
     VSAALKDPSY RLTTTTAEQI AARADPWDPS SVVTDNSDRD RLLTQAQAEL DRQIGLTRVK
     TQIERYRAAT MMAKVRAAKG MKVAQPSKHM IFTGPPGTGK TTIARVVANI LAGLGVISEP
     KLVETSRKDF VAEYEGQSAV KAAKTIDLAL GGVLFIDEAY ALVQERDGRT DPFGQEALDT
     LLARMENDRD RLVVIIAGYS SDIDRLLETN EGLRSRFATR IEFDTYSPDE LLEIAKVIAT
     DADSSLSAEA SKNLLEAAKQ LAQRTLRGRP ALDVAGNGRY ARQLVEAAEQ CRDMRLARGV
     DIEQLDVDRL QEINGSDMAE AIATVHAHLN IRE