ID   CWHA_ACHLY              Reviewed;         177 AA.
AC   P81717;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase A;
DE            EC=3.5.1.28;
GN   Name=cwhA;
OS   Achromobacter lyticus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=224;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, MASS SPECTROMETRY, AND DISULFIDE BOND.
RC   STRAIN=M497-1;
RX   PubMed=10833271; DOI=10.1093/oxfordjournals.jbchem.a022694;
RA   Li S., Norioka S., Sakiyama F.;
RT   "Purification, characterization, and primary structure of a novel cell wall
RT   hydrolytic amidase, CwhA, from Achromobacter lyticus.";
RL   J. Biochem. 127:1033-1039(2000).
CC   -!- FUNCTION: Antibacterial activity against Gram-positive bacteria
CC       M.luteus, S.aureus, E.faecalis and P.acidilactici and Gram-negative
CC       bacterium E.coli. {ECO:0000269|PubMed:10833271}.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- MASS SPECTROMETRY: Mass=19395.9; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:10833271};
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DR   PIR; JC7276; JC7276.
DR   AlphaFoldDB; P81717; -.
DR   SMR; P81717; -.
DR   BRENDA; 3.5.1.28; 74.
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:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; -; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; SSF55846; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Cell wall biogenesis/degradation;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Secreted.
FT   CHAIN           1..177
FT                   /note="N-acetylmuramoyl-L-alanine amidase A"
FT                   /id="PRO_0000079618"
FT   DOMAIN          23..158
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
FT   DISULFID        114..121
FT                   /evidence="ECO:0000269|PubMed:10833271"
SQ   SEQUENCE   177 AA;  19395 MW;  040D7F5D806C9C53 CRC64;
     AVDFGEAIWN PASSSNYSTA SNQTSAVIMH TMEGSYAGSI SWFQNPSAQV SAHYLIRKSD
     GQITQMVREY HQAWHAKNHN YYTIGIEHDG RAADAGNWSA AMVNASARLT KSICARRGVN
     CASAWKGPGY DTFHLVPDSV RVKGHGMLSG NENRYDPGKY FPWSNYYNLI NGGGGNP