ECCA2_MYCTO
ID ECCA2_MYCTO Reviewed; 619 AA.
AC P9WPH6; L0TDU9; O05460;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=ESX-2 secretion system protein EccA2;
DE AltName: Full=ESX conserved component A2;
DE AltName: Full=Type VII secretion system protein EccA2;
DE Short=T7SS protein EccA2;
GN Name=eccA2; OrderedLocusNames=MT3999;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- FUNCTION: Shows ATPase activity. Could provide energy for export of
CC ESX-2 substrates (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Part of the ESX-2 / type VII secretion system (T7SS), which is
CC composed of cytosolic and membrane components. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK48367.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000516; AAK48367.1; ALT_INIT; Genomic_DNA.
DR PIR; E70597; E70597.
DR RefSeq; WP_003400005.1; NZ_KK341228.1.
DR AlphaFoldDB; P9WPH6; -.
DR SMR; P9WPH6; -.
DR EnsemblBacteria; AAK48367; AAK48367; MT3999.
DR KEGG; mtc:MT3999; -.
DR PATRIC; fig|83331.31.peg.4303; -.
DR HOGENOM; CLU_008749_5_0_11; -.
DR Proteomes; UP000001020; 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.
FT CHAIN 1..619
FT /note="ESX-2 secretion system protein EccA2"
FT /id="PRO_0000426950"
FT BINDING 373..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 619 AA; 67969 MW; 3C40430D73E68C47 CRC64;
MSRMVDTMGD LLTARRHFDR AMTIKNGQGC VAALPEFVAA TEADPSMADA WLGRIACGDR
DLASLKQLNA HSEWLHRETT RIGRTLAAEV QLGPSIGITV TDASQVGLAL SSALTIAGEY
AKADALLANR ELLDSWRNYQ WHQLARAFLM YVTQRWPDVL STAAEDLPPQ AIVMPAVTAS
ICALAAHAAA HLGQGRVALD WLDRVDVIGH SRSSGRFGAD VLTAAIGPAD IPLLVADLAY
VRGMVYRQLH EEDKAQIWLS KATINGVLTD AAKEALADPN LRLIVTDERT IASRSDRWDA
STAKSRDQLD DDNAAQRRGE LLAEGRELLA KQVGLAAVKQ AVSALEDQLE VRMMRLEHGL
PVEGQTNHML LVGPPGTGKT TTAEALGKIY AGMGIVRHPE IREVRRSDFC GHYIGESGPK
TNELIEKSLG RIIFMDEFYS LIERHQDGTP DMIGMEAVNQ LLVQLETHRF DFCFIGAGYE
DQVDEFLTVN PGLAGRFNRK LRFESYSPVE IVEIGHRYAT PRASQLDDAA REVFLDAVTT
IRNYTTPSGQ HGIDAMQNGR FARNVIERAE GFRDTRVVAQ KRAGQPVSVQ DLQIITATDI
DAAIRSVCSD NRDMAAIVW