ID   Y2190_MYCTO             Reviewed;         385 AA.
AC   P9WHU2; L0TBK4; O53524; P67473; Q10383;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Probable endopeptidase MT2245;
DE            EC=3.4.-.-;
GN   OrderedLocusNames=MT2245;
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   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46531.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46531.1; ALT_INIT; Genomic_DNA.
DR   PIR; H70937; H70937.
DR   RefSeq; WP_003411373.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHU2; -.
DR   SMR; P9WHU2; -.
DR   EnsemblBacteria; AAK46531; AAK46531; MT2245.
DR   KEGG; mtc:MT2245; -.
DR   PATRIC; fig|83331.31.peg.2421; -.
DR   HOGENOM; CLU_034085_1_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS51935; NLPC_P60; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Thiol protease.
FT   CHAIN           1..385
FT                   /note="Probable endopeptidase MT2245"
FT                   /id="PRO_0000428122"
FT   DOMAIN          270..385
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   REGION          235..268
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..261
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        300
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        348
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        360
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   385 AA;  39756 MW;  0F8F26577D0468DA CRC64;
     MRLDQRWLIA RVIMRSAIGF FASFTVSSGV LAANVLADPA DDALAKLNEL SRQAEQTTEA
     LHSAQLDLNE KLAAQRAADQ KLADNRTALD AARARLATFQ TAVNKVAAAT YMGGRTHGMD
     AILTAESPQL LIDRLSVQRV MAHQMSTQMA RFKAAGEQAV KAEQAAAKSA ADARSAAEQA
     AAVRANLQHK QSQLQVQIAV VKSQYVALTP EERTALADPG PVPAVAAIAP GAPPAALPPG
     APPGDGPAPG VAPPPGGMPG LPFVQPDGAG GDRTAVVQAA LTQVGAPYAW GGAAPGGFDC
     SGLVMWAFQQ AGIALPHSSQ ALAHGGQPVA LSDLQPGDVL TFYSDASHAG IYIGDGLMVH
     SSTYGVPVRV VPMDSSGPIY DARRY