ID   ECCA5_MYCTU             Reviewed;         610 AA.
AC   P9WPI1; L0TAM8; O53947; P63744;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=ESX-5 secretion system protein EccA5 {ECO:0000305};
DE   AltName: Full=ESX conserved component A5 {ECO:0000303|PubMed:19876390};
DE   AltName: Full=Type VII secretion system protein EccA5 {ECO:0000305};
DE            Short=T7SS protein EccA5 {ECO:0000305};
GN   Name=eccA5 {ECO:0000303|PubMed:19876390}; OrderedLocusNames=Rv1798;
GN   ORFNames=MTV049.20;
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   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).
RN   [3]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=H37Rv;
RX   PubMed=22340629; DOI=10.1111/j.1365-2958.2012.08001.x;
RA   Bottai D., Di Luca M., Majlessi L., Frigui W., Simeone R., Sayes F.,
RA   Bitter W., Brennan M.J., Leclerc C., Batoni G., Campa M., Brosch R.,
RA   Esin S.;
RT   "Disruption of the ESX-5 system of Mycobacterium tuberculosis causes loss
RT   of PPE protein secretion, reduction of cell wall integrity and strong
RT   attenuation.";
RL   Mol. Microbiol. 83:1195-1209(2012).
RN   [5]
RP   FUNCTION.
RX   PubMed=22925462; DOI=10.1111/j.1365-2958.2012.08206.x;
RA   Houben E.N., Bestebroer J., Ummels R., Wilson L., Piersma S.R.,
RA   Jimenez C.R., Ottenhoff T.H., Luirink J., Bitter W.;
RT   "Composition of the type VII secretion system membrane complex.";
RL   Mol. Microbiol. 86:472-484(2012).
CC   -!- FUNCTION: Part of the ESX-5 specialized secretion system, which is
CC       responsible for the secretion of EsxN and a number of PE_PGRS and PPE
CC       proteins, including PPE41 (PubMed:22340629, PubMed:22925462). EccA5
CC       exhibits ATPase activity and may provide energy for the export of ESX-5
CC       substrates (By similarity). {ECO:0000250|UniProtKB:P9WPH9,
CC       ECO:0000269|PubMed:22340629, ECO:0000269|PubMed:22925462}.
CC   -!- SUBUNIT: Part of the ESX-5 / type VII secretion system (T7SS), which is
CC       composed of cytosolic and membrane components.
CC       {ECO:0000250|UniProtKB:P9WPH9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B2HSU9}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant does not secrete EsxN and shows a
CC       minor reduction of PPE41 secretion. {ECO:0000269|PubMed:22340629}.
CC   -!- SIMILARITY: Belongs to the CbxX/CfxQ family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44564.1; -; Genomic_DNA.
DR   PIR; G70930; G70930.
DR   RefSeq; NP_216314.1; NC_000962.3.
DR   RefSeq; WP_003408868.1; NZ_NVQJ01000037.1.
DR   AlphaFoldDB; P9WPI1; -.
DR   SMR; P9WPI1; -.
DR   STRING; 83332.Rv1798; -.
DR   iPTMnet; P9WPI1; -.
DR   PaxDb; P9WPI1; -.
DR   GeneID; 45425775; -.
DR   GeneID; 885543; -.
DR   KEGG; mtu:Rv1798; -.
DR   TubercuList; Rv1798; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0464; Bacteria.
DR   OMA; RTGRWPD; -.
DR   PhylomeDB; P9WPI1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
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; SSF48452; SSF48452; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR03922; T7SS_EccA; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Cytoplasm; Nucleotide-binding;
KW   Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:21969609"
FT   CHAIN           2..610
FT                   /note="ESX-5 secretion system protein EccA5"
FT                   /id="PRO_0000063046"
FT   BINDING         357..364
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylthreonine"
FT                   /evidence="ECO:0007744|PubMed:21969609"
SQ   SEQUENCE   610 AA;  67756 MW;  E6DE3C2D1C5356BC CRC64;
     MTRPQAAAED ARNAMVAGLL ASGISVNGLQ PSHNPQVAAQ MFTTATRLDP KMCDAWLARL
     LAGDQSIEVL AGAWAAVRTF GWETRRLGVT DLQFRPEVSD GLFLRLAITS VDSLACAYAA
     VLAEAKRYQE AAELLDATDP RHPFDAELVS YVRGVLYFRT KRWPDVLAQF PEATQWRHPE
     LKAAGAAMAT TALASLGVFE EAFRRAQEAI EGDRVPGAAN IALYTQGMCL RHVGREEEAV
     ELLRRVYSRD AKFTPAREAL DNPNFRLILT DPETIEARTD PWDPDSAPTR AQTEAARHAE
     MAAKYLAEGD AELNAMLGME QAKKEIKLIK STTKVNLARA KMGLPVPVTS RHTLLLGPPG
     TGKTSVARAF TKQLCGLTVL RKPLVVETSR TKLLGRYMAD AEKNTEEMLE GALGGAVFFD
     EMHTLHEKGY SQGDPYGNAI INTLLLYMEN HRDELVVFGA GYAKAMEKML EVNQGLRRRF
     STVIEFFSYT PQELIALTQL MGRENEDVIT EEESQVLLPS YTKFYMEQSY SEDGDLIRGI
     DLLGNAGFVR NVVEKARDHR SFRLDDEDLD AVLASDLTEF SEDQLRRFKE LTREDLAEGL
     RAAVAEKKTK