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Database: UniProt
Entry: A0A2A7N0L3_MYCAG
LinkDB: A0A2A7N0L3_MYCAG
Original site: A0A2A7N0L3_MYCAG 
ID   A0A2A7N0L3_MYCAG        Unreviewed;       280 AA.
AC   A0A2A7N0L3;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=CQY20_17090 {ECO:0000313|EMBL:PEG37071.1}, MAGR_35340
GN   {ECO:0000313|EMBL:GFG52093.1};
OS   Mycolicibacterium agri (Mycobacterium agri).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=36811 {ECO:0000313|EMBL:PEG37071.1, ECO:0000313|Proteomes:UP000220914};
RN   [1] {ECO:0000313|EMBL:PEG37071.1, ECO:0000313|Proteomes:UP000220914}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCUG37673 {ECO:0000313|EMBL:PEG37071.1,
RC   ECO:0000313|Proteomes:UP000220914};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GFG52093.1, ECO:0000313|Proteomes:UP000465302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG52093.1,
RC   ECO:0000313|Proteomes:UP000465302};
RX   PubMed=31287781;
RA   Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA   Iida T., Fujita J., Nakamura S.;
RT   "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT   species based on 7547 genomic profiles.";
RL   Emerg. Microbes Infect. 8:1043-1053(2019).
RN   [3] {ECO:0000313|EMBL:GFG52093.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG52093.1};
RA   Matsumoto Y., Motooka D., Nakamura S.;
RL   Submitted (FEB-2020) 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}.
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:PEG37071.1}.
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DR   EMBL; BLKS01000001; GFG52093.1; -; Genomic_DNA.
DR   EMBL; PDCP01000029; PEG37071.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A7N0L3; -.
DR   OrthoDB; 514320at2; -.
DR   Proteomes; UP000220914; Unassembled WGS sequence.
DR   Proteomes; UP000465302; 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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220914};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          86..226
FT                   /note="Peptidoglycan recognition protein family"
FT                   /evidence="ECO:0000259|SMART:SM00701"
FT   DOMAIN          96..233
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000259|SMART:SM00644"
FT   REGION          39..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        44..58
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   280 AA;  29511 MW;  E24C72A4BF66B70B CRC64;
     MDVAAASPNQ RGQALSRRRL LQLAGFAGIG LAAAGACSTK PAAEPSAPPS PPMPSAAPPS
     TVTTVIETAP PAPVVAPAPA VVPASNLMLC RDAWQASAPR PGGTPHQLSS MTIHHTAVVL
     GANENAPRRL RQHQRYHQDT HGWIDIAYHL SVDRNGNIYE LRDPQLVGDT ATSYDPTGHF
     LVVCEGDFDQ EEISEDQLNG AALAFAWAAE QYNIPTDRLA GHKDESGDTA CPGASLYAHV
     TSGELQRRID AILANGPVNL QKICGPEATA YVADIEAGIR
//
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