ID   CWLX_BACLI              Reviewed;         354 AA.
AC   Q99125;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Probable N-acetylmuramoyl-L-alanine amidase;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
DE   AltName: Full=ORFL3;
DE   Flags: Precursor;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MC14;
RX   PubMed=2033382; DOI=10.1099/00221287-137-3-667;
RA   Lee J.W.K., Edwards C.W., Hulett F.M.;
RT   "Identification of four unique clones encoding 10 kDa proteins from
RT   Bacillus that cause phenotypic complementation of a phoA mutant strain of
RT   Escherichia coli.";
RL   J. Gen. Microbiol. 137:667-677(1991).
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; M63942; AAA22888.1; -; Genomic_DNA.
DR   PIR; D49754; D49754.
DR   AlphaFoldDB; Q99125; -.
DR   SMR; Q99125; -.
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; 1.10.101.10; -; 2.
DR   Gene3D; 3.40.80.10; -; 1.
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   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 2.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF47090; SSF47090; 2.
DR   SUPFAM; SSF55846; SSF55846; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..39
FT                   /evidence="ECO:0000250"
FT   CHAIN           40..354
FT                   /note="Probable N-acetylmuramoyl-L-alanine amidase"
FT                   /id="PRO_0000006456"
FT   DOMAIN          40..152
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  38347 MW;  9A84D197B73B52CD CRC64;
     MVKVINNFVK VNQYDRPGLK LAAVKGIVMH WTATPGASAL NERNYFNGTC IADKRYASAH
     YFVDRHEAQH IIPDHEVAYH AHDQNRCYVS FLKPNANTTA LGVEMCVEKD GTIHEETIRN
     AAELVADLCK TYGLSADRIV RHYDVTNKGC PTPWVRDAGQ LSAFRKRVDS LLGRKTVSVS
     AASTSQTSSS SGIILKKGMS GSHVKKLQTR LVAAGFSLPK YGADGSYGDE TVHAVVSLQK
     KAGIKADGIY GPSTEKALSA AEASAAGKSK TWTLPDGIYK VKNPLMKGTA VTQIQTALAA
     LYYYPDKGAK NNGIDGYYGM KTANAVKRFQ LMYGLGADGI YGPKTKAKML SLLK