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Database: UniProt
Entry: A0A1H0AA71_9FIRM
LinkDB: A0A1H0AA71_9FIRM
Original site: A0A1H0AA71_9FIRM 
ID   A0A1H0AA71_9FIRM        Unreviewed;       165 AA.
AC   A0A1H0AA71;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=SAMN04488502_11710 {ECO:0000313|EMBL:SDN30191.1};
OS   Dendrosporobacter quercicolus.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Dendrosporobacter.
OX   NCBI_TaxID=146817 {ECO:0000313|EMBL:SDN30191.1, ECO:0000313|Proteomes:UP000214880};
RN   [1] {ECO:0000313|EMBL:SDN30191.1, ECO:0000313|Proteomes:UP000214880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1736 {ECO:0000313|EMBL:SDN30191.1,
RC   ECO:0000313|Proteomes:UP000214880};
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};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007553}.
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DR   EMBL; FNHB01000017; SDN30191.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0AA71; -.
DR   STRING; 146817.SAMN04488502_11710; -.
DR   OrthoDB; 9812621at2; -.
DR   Proteomes; UP000214880; Unassembled WGS sequence.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; 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   InterPro; IPR015510; PGRP.
DR   InterPro; IPR006619; PGRP_domain_met/bac.
DR   PANTHER; PTHR11022; PEPTIDOGLYCAN RECOGNITION PROTEIN; 1.
DR   PANTHER; PTHR11022:SF41; PEPTIDOGLYCAN-RECOGNITION PROTEIN SC1A-RELATED; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SMART; SM00701; PGRP; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214880};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          9..139
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   DOMAIN          11..133
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
SQ   SEQUENCE   165 AA;  18402 MW;  A8B4B0CEA9C1F431 CRC64;
     MIDVKETYLT FGDMVPQSVV KMIIIHHVGD LPRDVAAAEI HQWHLDRGWS GIGYHYVIRR
     DGSIERGRPE EYIGSHTYGY NTGSIGINLA GNMEIMTPAK AQIESAAMLI ADVCNRYDLT
     PDSKTVLGHR DLTSTACPGK NLYEQLQTIR GKAVWYQHNG SGEEV
//
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