ID   CWLL_BACLI              Reviewed;         360 AA.
AC   P36550;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-MAY-2023, entry version 88.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase CwlL;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
DE   Flags: Precursor;
GN   Name=cwlL;
OS   Bacillus licheniformis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FD0120;
RX   PubMed=7902527; DOI=10.1007/bf00284691;
RA   Oda Y., Nakayama R., Kuroda A., Sekiguchi J.;
RT   "Molecular cloning, sequence analysis, and characterization of a new cell
RT   wall hydrolase, CwlL, of Bacillus licheniformis.";
RL   Mol. Gen. Genet. 241:380-388(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; D13377; BAA02647.1; -; Genomic_DNA.
DR   PIR; S39916; S39916.
DR   AlphaFoldDB; P36550; -.
DR   SMR; P36550; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 2.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 2.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 2.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Repeat; Secreted; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000250"
FT   CHAIN           40..360
FT                   /note="N-acetylmuramoyl-L-alanine amidase CwlL"
FT                   /id="PRO_0000006455"
FT   DOMAIN          40..154
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   REPEAT          166..191
FT                   /note="1-1"
FT   REPEAT          196..259
FT                   /note="2-1"
FT   REPEAT          265..289
FT                   /note="1-2"
FT   REPEAT          291..355
FT                   /note="2-2"
FT   REGION          166..289
FT                   /note="2 X approximate repeats"
FT   REGION          196..355
FT                   /note="2 X approximate repeats"
SQ   SEQUENCE   360 AA;  38996 MW;  37C07B4A084364DA CRC64;
     MVKVVKNFVK VNQYTRPGLK LAGVKGIVMH YTATPGASAL NERDYFNGTC IAIKRKASSA
     HYFVDRKEAQ HIIPENEVAY HAHDKNRCYV SFLKPNANTK SISVEMCVEK DGMIHSETVQ
     NAAELVADLC KRYGLSTNKI VRHYDVTNKI CPAPWVSDSS QLTTFRKKVD SLLGNKTVSK
     TTSSTSQSSK STGTILKKGA SGSQVKALQK RLIAAGFSLP KYGADGSYEN ETVQAVKALQ
     KKAGIAVDGI YGPATEKALA AIGAKKKKPS SNGKKTSYPL PSGIYKVKSP LMKGTGVRQI
     QEALAALYFY PDKGAKNNGI DGYYGPKTAN AVKRFQLMHG LSADGIYGSD TKAKLKTLLK
//