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Database: UniProt
Entry: A0A1I0QID5_9GAMM
LinkDB: A0A1I0QID5_9GAMM
Original site: A0A1I0QID5_9GAMM 
ID   A0A1I0QID5_9GAMM        Unreviewed;       260 AA.
AC   A0A1I0QID5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=SAMN04515660_3471 {ECO:0000313|EMBL:SEW26932.1};
OS   Luteibacter sp. 329MFSha.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Luteibacter.
OX   NCBI_TaxID=1798239 {ECO:0000313|EMBL:SEW26932.1, ECO:0000313|Proteomes:UP000199162};
RN   [1] {ECO:0000313|EMBL:SEW26932.1, ECO:0000313|Proteomes:UP000199162}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=329MFSha {ECO:0000313|EMBL:SEW26932.1,
RC   ECO:0000313|Proteomes:UP000199162};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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};
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DR   EMBL; FOJE01000005; SEW26932.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I0QID5; -.
DR   STRING; 1798239.SAMN04515660_3471; -.
DR   Proteomes; UP000199162; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF10; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..260
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011486567"
FT   DOMAIN          44..177
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
SQ   SEQUENCE   260 AA;  28127 MW;  10D9EFB5E419F4DE CRC64;
     MTPRHAIVAR RTVRAAVVLA MATLAGCASA PRVAPQRSPI AHWTPSPNYN ARKAQIIVLH
     HTSIGNATEA LRVLSTRNSE GQVSAHYLVE SDGRIDQLVD DGDRAWHAGA SRWGDMTDLN
     SSSIGIEIDN DGESPFTDAQ IQALIRLLAD LTSRLGIPRQ AVVGHGDIAP GRKTDPSAQF
     PWATLARYGF GLWPDAVLVP APPGFDSLAA LRLVGYDVST PRTAIAAFHR HYRAMETDTL
     DATDAAILYS LQRKLMAPRQ
//
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