ID   A0A0F2S593_9RHOB        Unreviewed;       412 AA.
AC   A0A0F2S593;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=VR71_02770 {ECO:0000313|EMBL:KJS45340.1};
OS   Roseovarius sp. BRH_c41.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=1629709 {ECO:0000313|EMBL:KJS45340.1, ECO:0000313|Proteomes:UP000033676};
RN   [1] {ECO:0000313|EMBL:KJS45340.1, ECO:0000313|Proteomes:UP000033676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c41 {ECO:0000313|EMBL:KJS45340.1};
RA   Bagnoud A., Chourey K., Hettich R.L., de Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00001561};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KJS45340.1}.
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DR   EMBL; LADY01000007; KJS45340.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F2S593; -.
DR   PATRIC; fig|1629709.5.peg.4905; -.
DR   Proteomes; UP000033676; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 2.60.40.3500; -; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR021731; AMIN_dom.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF11741; AMIN; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..412
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002458515"
FT   DOMAIN          242..397
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
SQ   SEQUENCE   412 AA;  43621 MW;  F836771062EE734C CRC64;
     MSRTLGIVLA MALAFAGLTG ARAQDATFSG LARLDVAASA ITDTGQGVDV HLRLSQGVPY
     RVYTLSDPAR LVLDFKEVDW QGVGAADLIR GERVKGLRLG QIRPGWSRMV ADLDAPYPLA
     RAGLDIDNAS GAADLRVRLG AADATRFAAT AGTPDLPGWD MPDPQSGLAA APGRVPGEGP
     LMVVLDPGHG GIDPGAQEGE LAEKTLMLQF AQELREELLR AGGFDVILTR DSDEFVSLER
     RVALAHWAGA DVFLSLHADA LTGAQARGLS VYTLSESASD EASAALAERH NRADMLAGVD
     LSGKDDIVAD VLMDLARIET RPRTEQLATA LIESFAAHEL PLLSRPLRHA GFSVLKAPDI
     PSALIELGFL SSPRDLARLR NAEGRARIAT ALRAGLMAWR DADAARAGLV RQ
//