ID   Y2190_MYCTU             Reviewed;         385 AA.
AC   P9WHU3; 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 36.
DE   RecName: Full=Probable endopeptidase Rv2190c;
DE            EC=3.4.-.-;
GN   OrderedLocusNames=Rv2190c; ORFNames=MTCY190.01c, MTV021.23c;
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).
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
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DR   EMBL; AL123456; CCP44967.1; -; Genomic_DNA.
DR   PIR; H70937; H70937.
DR   RefSeq; NP_216706.1; NC_000962.3.
DR   RefSeq; WP_003411373.1; NZ_NVQJ01000008.1.
DR   AlphaFoldDB; P9WHU3; -.
DR   SMR; P9WHU3; -.
DR   STRING; 83332.Rv2190c; -.
DR   PaxDb; P9WHU3; -.
DR   DNASU; 888670; -.
DR   GeneID; 888670; -.
DR   KEGG; mtu:Rv2190c; -.
DR   TubercuList; Rv2190c; -.
DR   eggNOG; COG0791; Bacteria.
DR   OMA; GYAMQFQ; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005576; C:extracellular region; HDA:MTBBASE.
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; Reference proteome; Thiol protease.
FT   CHAIN           1..385
FT                   /note="Probable endopeptidase Rv2190c"
FT                   /id="PRO_0000109873"
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