ID A0A143QDP2_9NOCA Unreviewed; 691 AA.
AC A0A143QDP2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=A3Q40_03650 {ECO:0000313|EMBL:AMY21004.1};
OS Rhodococcus sp. PBTS 1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1653478 {ECO:0000313|EMBL:AMY21004.1, ECO:0000313|Proteomes:UP000076180};
RN [1] {ECO:0000313|EMBL:AMY21004.1, ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|EMBL:AMY21004.1,
RC ECO:0000313|Proteomes:UP000076180};
RX PubMed=27284129;
RA Stamler R.A., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus Isolates PBTS 1 and PBTS 2.";
RL Genome Announc. 4:0-0(2016).
RN [2] {ECO:0000313|Proteomes:UP000076180}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBTS 1 {ECO:0000313|Proteomes:UP000076180};
RA Stamer R., Vereecke D., Zhang Y., Schilkey F., Devitt N., Randall J.;
RT "Complete Genome and Plasmid Sequences for Rhodococcus fascians D188 and
RT Draft Sequences for Rhodococcus spp. Isolates PBTS 1 and PBTS 2.";
RL Submitted (APR-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; CP015219; AMY21004.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A143QDP2; -.
DR STRING; 1653478.A3Q40_03650; -.
DR KEGG; rhu:A3Q40_03650; -.
DR PATRIC; fig|1653478.3.peg.3705; -.
DR Proteomes; UP000076180; Chromosome.
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:UP000076180};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 294..442
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 307..471
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 158..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..691
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..233
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..691
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 70616 MW; BD90070473FCFD16 CRC64;
MHRRPKPALV MGVVAALAVT TPVAVHLVRQ QHTDVQTATD SAVVVPTQIA KLALASAPDI
VIPLEELTGL PLPDIDLGSL RDLPIPDNLE IPAIPGLTAP VAPAPLAPGD VAGAVEIPAN
GAVVKEVAQD TPFSMVALTA EQLGNAVARV RAQLEDGSWG PWNETQPIDT GRSDSDVPTA
AAGTEPIYVG ETKRVQFLLT PTVPTPAANP ADPAFPVPPA PAPADPVPAP AEPARPAADL
GYIPASSSSP LRTQPADQSA QTLADAAAVL ITPGTSAADA TLTDIATPLA GSGPAVISRA
QWGADESIRC GSPTYDDSLG GATIHHTAGS NDYTRQESAG IVRAIYAYHA KTLGWCDIGY
NVLVDKYGQI FEGRAGGLDR NVEGAHAGGF NENTMGLALM GDYSRVAPTQ ESIDAAGRFL
GWRLGKAGLD PMGRTTMYSE GTQYTFVPQG NAIDLPVIFA HRDVGNTECP GDAAYARLGD
IRTIAAANLG GGTTTSPVTS PDTVVGGGTV PAPPSTDASG RDSSAALRGL VSDLLRMGVQ
NPVVQKWVAE GGESGRLGAA LTGLLPIADG LEKADFVNGS IYTTPTGQVV SVLGKIYQQF
VAQGSESGSL GLPTTDEYDI PGGKQTDFTN GSLIFDQVTG IVTTVMKTFV DTYTTEMNAG
APAAPAPEAA PAPEAAPAPE AAPAPEPAPV G
//