ID W5T6L9_9NOCA Unreviewed; 759 AA.
AC W5T6L9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=NONO_c01300 {ECO:0000313|EMBL:AHH14950.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH14950.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH14950.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH14950.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(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; CP006850; AHH14950.1; -; Genomic_DNA.
DR AlphaFoldDB; W5T6L9; -.
DR STRING; 1415166.NONO_c01300; -.
DR KEGG; nno:NONO_c01300; -.
DR PATRIC; fig|1415166.3.peg.127; -.
DR eggNOG; COG5479; Bacteria.
DR HOGENOM; CLU_018529_1_0_11; -.
DR Proteomes; UP000019150; 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 PRINTS; PR01217; PRICHEXTENSN.
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:UP000019150};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..759
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004871735"
FT DOMAIN 293..441
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 307..470
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 97..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 205..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..759
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..668
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 675..697
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..732
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..759
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 759 AA; 78054 MW; EBDDEBFEB91E9CC3 CRC64;
MPYRRPKRSV VLPVVATLAV AAPLATLTLH DSPGYRMADD SNLAAIPAEL AEVALSSAPD
VVLPLRELTG LNLPDLHLSD LRKLPLPKAI PVPPGLPAPP GVRLPSEIPL PQFGDRSDAP
APQPAHSGPG FIAAPLDPAQ VPDGDPSEPA LAPGAVPPDL SDQVGAEVKQ LTRDTPFSMV
ALTADQLADT TSLIRAQQAD GTWGAWYPTD QVDTNRDDRS PAPARTGTEP IYVGATKAVQ
VLTTHKVAAP AAGRSDDPAQ AADQLSAVLI DPGRGAIDDK LSSVAAPLPG GGPKVISRAQ
WGADESLRCE EPTYDDGLGG ITVHHTAGRN DYSKSESAGI VRAIYAYHAK TLGWCDIGYN
ALVDKYGQIF EGRYGGMDRP VEGAHAGGFN ENTAGVAMMG DFESQPPTDA QLQATGQYVG
WRAKVAGLDP EGHTTMYSEG TDFTPYAEGE AVQLPIVFAH RDVGNTTCPG DAAYARMDQI
RQIAAGVTAG APSEAKKQGP RTDLAALANL TSQLLGMVDK NIIAKYWAAQ GGPNGRLGAV
AAEPAPTHDG GQYAKFVNGY VYAAPDGAIT ELAGRILDRF EQLGSDTGLL GTPQRSTYPV
PGGERADFQL GSLILNTATG VVTTLLKHSG PQQNPSADPI PAPLPDAAGP QAPSQPAAPA
PGPVTPEAQG APPVEGQVAP PPEPQAAPVP EAQAPGPEAT APAPEAQTPG PEAQAPGPDA
QAAPPPESQA PAPDSQTAPA PEAQAPDPQP APEAPAPEA
//
