ECCA2_MYCTU
ID ECCA2_MYCTU Reviewed; 619 AA.
AC P9WPH7; L0TDU9; O05460;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 40.
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=Rv3884c; ORFNames=MTCY15F10.28;
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 GENE NAME.
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).
RN [3]
RP SUBUNIT.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19854905; DOI=10.1128/jb.01032-09;
RA Callahan B., Nguyen K., Collins A., Valdes K., Caplow M., Crossman D.K.,
RA Steyn A.J., Eisele L., Derbyshire K.M.;
RT "Conservation of structure and protein-protein interactions mediated by the
RT secreted mycobacterial proteins EsxA, EsxB, and EspA.";
RL J. Bacteriol. 192:326-335(2010).
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: 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 (By similarity). Residues
CC 522-619 interact with an artificial EsxB-EsxA heterodimer from the
CC adjacent ESX-1 locus (PubMed:19854905). {ECO:0000250,
CC ECO:0000269|PubMed:19854905}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46713.1; -; Genomic_DNA.
DR PIR; E70597; E70597.
DR RefSeq; NP_218401.1; NC_000962.3.
DR RefSeq; WP_003907154.1; NZ_NVQJ01000082.1.
DR AlphaFoldDB; P9WPH7; -.
DR SMR; P9WPH7; -.
DR STRING; 83332.Rv3884c; -.
DR PaxDb; P9WPH7; -.
DR DNASU; 886210; -.
DR GeneID; 886210; -.
DR KEGG; mtu:Rv3884c; -.
DR TubercuList; Rv3884c; -.
DR eggNOG; COG0464; Bacteria.
DR OMA; PPQAIIM; -.
DR PhylomeDB; P9WPH7; -.
DR Proteomes; UP000001584; 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; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome.
FT CHAIN 1..619
FT /note="ESX-2 secretion system protein EccA2"
FT /id="PRO_0000063051"
FT BINDING 373..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 619 AA; 68041 MW; 8BA2EAD3CCCEF09B CRC64;
MSRMVDTMGD LLTARRHFDR AMTIKNGQGC VAALPEFVAA TEADPSMADA WLGRIACGDR
DLASLKQLNA HSEWLHRETT RIGRTLAAEV QLGPSIGITV TDASQVGLAL SSALTIAGEY
AKADALLANR ELLDSWRNYQ WHQLARAFLM YVTQRWPDVL STAAEDLPPQ AIVMPAVTAS
ICALAAHAAA HLGQGRVALD WLDRVDVIGH SRSSERFGAD 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
