ID V9XIV5_9NOCA Unreviewed; 714 AA.
AC V9XIV5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=Y013_17395 {ECO:0000313|EMBL:AHD22288.1};
OS Rhodococcus pyridinivorans SB3094.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1435356 {ECO:0000313|EMBL:AHD22288.1, ECO:0000313|Proteomes:UP000018781};
RN [1] {ECO:0000313|EMBL:AHD22288.1, ECO:0000313|Proteomes:UP000018781}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB3094 {ECO:0000313|EMBL:AHD22288.1,
RC ECO:0000313|Proteomes:UP000018781};
RX PubMed=24874690;
RA Dueholm M.S., Albertsen M., D'Imperio S., Tale V.P., Lewis D.,
RA Nielsen P.H., Nielsen J.L.;
RT "Complete Genome of Rhodococcus pyridinivorans SB3094, a Methyl-Ethyl-
RT Ketone-Degrading Bacterium Used for Bioaugmentation.";
RL Genome Announc. 2:e00525-14(2014).
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; CP006996; AHD22288.1; -; Genomic_DNA.
DR RefSeq; WP_024102670.1; NC_023150.1.
DR AlphaFoldDB; V9XIV5; -.
DR GeneID; 29939151; -.
DR KEGG; rpy:Y013_17395; -.
DR PATRIC; fig|1435356.3.peg.3511; -.
DR eggNOG; COG5479; Bacteria.
DR HOGENOM; CLU_018529_1_0_11; -.
DR Proteomes; UP000018781; 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; IPR013207; LGFP.
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 Pfam; PF08310; LGFP; 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 Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..714
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038835040"
FT DOMAIN 299..447
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 312..476
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 137..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..235
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..530
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 689..714
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 714 AA; 73390 MW; 545CC299E585796C CRC64;
MPHRRPKPSI VLGAVAALAV ATPFAVTGLT STAPEIRNAN DTVEAVAPDI AEVVLASVPD
LIIPLEELTG LNLPDLSLKE IVDGLPQITT APDPNGGLVQ RVGATVKELT RDTPFSLVAL
AAEDVAATDA LIRAQQDDGS WGPWTATEPI ETRADDATSE GRTGTEPIYV GATRAVQVLL
TPRPGPEPNL AGAEAPPAPE APAPTPEAPA PEAPAPEAPA PAAPAEAPVP ADEAPAPVAA
PAADAPDLGY VPASSSKPLR ENPLQAAAEA VSAVLISPGS SEADARLEDI ASPLGNSGLK
VITRQQWGAD ESMRCQTPTY DDSLGGATVH HTAGSNNYSK AESAEIVRAI YAYHARTLGW
CDIGYNTLVD KYGQIFEGRA GGLDRNVQGA HAGGFNENTH GIAMMGDFST QAPPQAAVES
VGKFLGWRLA RAGLNPKGRT TMYSEGTSFT PYPQGAAVDL PIIFAHRDVG NTSCPGDAGY
SQMGKIRDIA VAAAKGGGGG TAPQPSNPSP SNPQPSNPQP SNPSPSNPSP NVPDINVGAL
ASGSAGTAEG VVDELIRLSG HPLVQKWLAE GGELGRLGQA VTSILPAVKS GFERVNFVNG
AIYTSPNGGT WTVLGEIYKA WEKNGLDAGE LGLPTSDEYR VPDGWRSDFE FGSLIFNEVT
GVVTKVLRAY DDAYDQAMQD QPADVAGPAP EGAPAPGPEP APAPEPAPEP APAG
//
