ID   RIPB_MYCTO              Reviewed;         241 AA.
AC   P9WHU4; L0T9R3; O53169; Q7D8D5;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=Peptidoglycan endopeptidase RipB;
DE            EC=3.4.-.-;
DE   AltName: Full=Macrophage invasion and intracellular persistence protein B;
DE   AltName: Full=Resuscitation-promoting factor interaction partner B;
DE            Short=Rpf-interacting protein B;
DE   Flags: Precursor;
GN   Name=ripB; OrderedLocusNames=MT1525;
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: Peptidoglycan endopeptidase that cleaves the bond between D-
CC       glutamate and meso-diaminopimelate. Binds high-molecular weight
CC       peptidoglycan, but does not degrade it. Required for normal separation
CC       of daughter cells after cell division and cell wall integrity. Required
CC       for host cell invasion (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
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DR   EMBL; AE000516; AAK45790.1; -; Genomic_DNA.
DR   PIR; A70874; A70874.
DR   RefSeq; WP_003407525.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WHU4; -.
DR   SMR; P9WHU4; -.
DR   MEROPS; C40.012; -.
DR   PRIDE; P9WHU4; -.
DR   EnsemblBacteria; AAK45790; AAK45790; MT1525.
DR   GeneID; 45425457; -.
DR   KEGG; mtc:MT1525; -.
DR   PATRIC; fig|83331.31.peg.1640; -.
DR   HOGENOM; CLU_100951_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; 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   Cell wall biogenesis/degradation; Hydrolase; Protease; Signal;
KW   Thiol protease.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..241
FT                   /note="Peptidoglycan endopeptidase RipB"
FT                   /id="PRO_0000428121"
FT   DOMAIN          109..241
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        152
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        201
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        213
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   241 AA;  24624 MW;  C4DFAA6A4863BA7A CRC64;
     MRHTRFHPIK LAWITAVVAG LMVGVATPAD AEPGQWDPTL PALVSAGAPG DPLAVANASL
     QATAQATQTT LDLGRQFLGG LGINLGGPAA SAPSAATTGA SRIPRANARQ AVEYVIRRAG
     SQMGVPYSWG GGSLQGPSKG VDSGANTVGF DCSGLVRYAF AGVGVLIPRF SGDQYNAGRH
     VPPAEAKRGD LIFYGPGGGQ HVTLYLGNGQ MLEASGSAGK VTVSPVRKAG MTPFVTRIIE
     Y