ID   NAAA_LYSSP              Reviewed;          13 AA.
AC   P85143;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   11-DEC-2019, entry version 17.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase L2;
DE            EC=3.5.1.28;
DE   Flags: Fragment;
OS   Lysobacter sp.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter; unclassified Lysobacter.
OX   NCBI_TaxID=72226;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=XL1 {ECO:0000269|Ref.1};
RA   Muranova T.A., Stepnaya O.A., Tsfasman I.M., Kulaev I.S.;
RT   "Identification of extracellular bacteriolytic enzymes from Lysobacter sp.
RT   XL1.";
RL   Submitted (APR-2007) to UniProtKB.
CC   -!- FUNCTION: Has bacteriolytic activity. {ECO:0000269|Ref.1}.
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         Evidence={ECO:0000269|Ref.1};
CC   -!- ACTIVITY REGULATION: Inhibited by phenylmethanesulfonyl fluoride (PMSF)
CC       and EDTA. {ECO:0000269|Ref.1}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.0. {ECO:0000269|Ref.1};
CC       Temperature dependence:
CC         Optimum temperature is 65 degrees Celsius. {ECO:0000269|Ref.1};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|Ref.1}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
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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:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Direct protein sequencing; Hydrolase; Secreted.
FT   CHAIN           1..>13
FT                   /note="N-acetylmuramoyl-L-alanine amidase L2"
FT                   /id="PRO_0000287396"
FT   NON_TER         13
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   13 AA;  1547 MW;  49FA0BA84E42E447 CRC64;
     XNVVFLNXPX PQW