ID   CWLA_BACSP              Reviewed;         251 AA.
AC   P14892;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-MAY-2023, entry version 90.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase CwlA;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
DE   Flags: Precursor;
GN   Name=cwlA;
OS   Bacillus sp.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3070348; DOI=10.1007/bf00337717;
RA   Potvin C., Leclerc D., Tremblay G., Asselin A., Bellemare G.;
RT   "Cloning, sequencing and expression of a Bacillus bacteriolytic enzyme in
RT   Escherichia coli.";
RL   Mol. Gen. Genet. 214:241-248(1988).
CC   -!- FUNCTION: Autolysins are involved in some important biological
CC       processes such as cell separation, cell-wall turnover, competence for
CC       genetic transformation, formation of the flagella and sporulation.
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   -!- MISCELLANEOUS: Retention of enzymatic activity was limited to the N-
CC       terminal fragment (AA 1-196).
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; X13524; CAA31877.1; -; Genomic_DNA.
DR   PIR; S08306; S08306.
DR   AlphaFoldDB; P14892; -.
DR   SMR; P14892; -.
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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR021976; Amidase_C.
DR   InterPro; IPR002502; Amidase_domain.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF11; N-ACETYLMURAMOYL-L-ALANINE AMIDASE XLYA; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF12123; CBD_PlyG; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   3: Inferred from homology;
KW   Antimicrobial; Bacteriolytic enzyme; Cell wall biogenesis/degradation;
KW   Competence; Hydrolase; Secreted; Signal; Sporulation.
FT   SIGNAL          1..37
FT   CHAIN           38..251
FT                   /note="N-acetylmuramoyl-L-alanine amidase CwlA"
FT                   /id="PRO_0000006452"
FT   DOMAIN          38..140
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   251 AA;  28473 MW;  1F52F36B20576F0D CRC64;
     MEIKQMLVPV SRYSVLCPYE MNPTEITFHN TYNDAPAINE RNNVANNSTG TSFHIAVDDK
     EAIQLIPFNR NAWHAGDGTN GRGNRHSIGV EICYSQSGGA RYRKAELNAV EVIAQLMIQF
     DIPISKVKTH QERNGKYCPH RMLDEGRVQW FKNQCANRAS SIKNSNKTQE TGKVEIIVNK
     FNKVVTYEFG TALVPEMLGM MDALGYESRI ISYGDKQGLV RFETAYRQGN ELDKATAWLD
     AKGLKYFYTK E
//