ID   CWLO_BACLD              Reviewed;         452 AA.
AC   Q65NQ9; Q62Z56;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Peptidoglycan DL-endopeptidase CwlO;
DE            EC=3.4.-.-;
DE   AltName: Full=D-gamma-glutamyl-meso-diaminopimelyl DL-endopeptidase;
DE   Flags: Precursor;
GN   Name=cwlO; OrderedLocusNames=BLi00347, BL01691;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
CC   -!- FUNCTION: Shows a cell wall hydrolytic DL-endopeptidase activity.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
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DR   EMBL; AE017333; AAU39305.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU21952.1; -; Genomic_DNA.
DR   RefSeq; WP_003178705.1; NC_006322.1.
DR   AlphaFoldDB; Q65NQ9; -.
DR   SMR; Q65NQ9; -.
DR   STRING; 279010.BL01691; -.
DR   MEROPS; C40.010; -.
DR   PRIDE; Q65NQ9; -.
DR   EnsemblBacteria; AAU21952; AAU21952; BL01691.
DR   GeneID; 66217497; -.
DR   KEGG; bld:BLi00347; -.
DR   KEGG; bli:BL01691; -.
DR   eggNOG; COG0791; Bacteria.
DR   eggNOG; COG3883; Bacteria.
DR   HOGENOM; CLU_034085_0_1_9; -.
DR   OMA; GYAMQFQ; -.
DR   OrthoDB; 682655at2; -.
DR   BioCyc; BLIC279010:BLI_RS01705-MON; -.
DR   Proteomes; UP000000606; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; Reference proteome;
KW   Secreted; Signal; Thiol protease.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..452
FT                   /note="Peptidoglycan DL-endopeptidase CwlO"
FT                   /id="PRO_0000223367"
FT   DOMAIN          321..450
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   REGION          28..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          258..317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        258..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        273..317
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        358
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        410
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        422
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ   SEQUENCE   452 AA;  49109 MW;  9710E915FB158D79 CRC64;
     MKKKVYTFGL ASILGTASLF TPFMNNTASA ETSQQKQEIQ QKRSEVNSGI ESKRKEIAKL
     QDEQKKLEGK IQELDKKALE TSNKIEDKEK ENKKTKKEVE ALKKEIKETE KRIEERSKVI
     KNRVRSLQEN GGSQNYLNVL LGAQSFGDFI TRATAVSTIV DADKDLLDEQ EKDKNKLEKA
     MSDLNTKLDE IQKTLADLKT LKSDLDKQLK EQANLSKQLQ TKQAAAESEL SDLKKEAGSL
     TKEEAALEQK LKEERAAAAA AAKAKEESAT AEKSDSGSSS SSNSGSVSKS DGSSNSGSSS
     SKKSSSPSRN YSSGSVVSSN GNAIEAAIST GSSIVGRSPY KWGGGRSQAD IDNRRFDCSS
     FVRWAYASAG VELGFGATTS TLVGKGRAVS ASEMKRGDLV FFDTYKTNGH VGIYLGNGTF
     LNDNSSRGVS VDSMSNPYWK KAFNGVVRRV VE