GenomeNet

Database: UniProt
Entry: A0A143QDP2_9NOCA
LinkDB: A0A143QDP2_9NOCA
Original site: A0A143QDP2_9NOCA 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system