ID I0L311_9ACTN Unreviewed; 376 AA.
AC I0L311;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=MILUP08_43113 {ECO:0000313|EMBL:CCH18208.1};
OS Micromonospora lupini str. Lupac 08.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1150864 {ECO:0000313|EMBL:CCH18208.1, ECO:0000313|Proteomes:UP000003448};
RN [1] {ECO:0000313|Proteomes:UP000003448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lupac 08 {ECO:0000313|Proteomes:UP000003448};
RX PubMed=22815450; DOI=10.1128/jb.00628-12;
RA Alonso-Vega P., Normand P., Bacigalupe R., Pujic P., Lajus A., Vallenet D.,
RA Carro L., Coll P., Trujillo M.E.;
RT "Genome Sequence of Micromonospora lupini Lupac 08, Isolated from Root
RT Nodules of Lupinus angustifolius.";
RL J. Bacteriol. 194:4135-4135(2012).
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:CCH18208.1}.
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DR EMBL; CAIE01000025; CCH18208.1; -; Genomic_DNA.
DR AlphaFoldDB; I0L311; -.
DR STRING; 1150864.MILUP08_43113; -.
DR eggNOG; COG3023; Bacteria.
DR eggNOG; COG3409; Bacteria.
DR OrthoDB; 514320at2; -.
DR Proteomes; UP000003448; 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 Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 2.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
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 Pfam; PF01471; PG_binding_1; 2.
DR SMART; SM00644; Ami_2; 1.
DR SMART; SM00701; PGRP; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 2.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000003448};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 47..199
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 57..205
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 376 AA; 40878 MW; AB5D680F4CBEC99E CRC64;
MHVDHSEVDR RTLLRAGLGA ATVAVVGSEL AFSGAAQAAP GTDLDWIISC DEWAARPPKD
PLSVSAIATN KIIVHHMAFP NVTDYSREQA VKLAHDCQDL HIDGNGWSDT GQHFTVSRGG
YVLEGRRGSL ERLEAGDRQM ISAHCPGENG RAIGIENEGT YVTETPPEAL TDSLVKLCVT
ICRQYGLHAF DIFGHWDFRT TDCPGAAFYR QFPALRRRVH AALGTKLGDV PARRWPDLWR
FVNSPSVRVV QHLLAYRGYA VTVSGTFDAA TVAAVQDWQA RNGIAVDVDA TLTTPTWETL
APELDQHAVG APVTAVQEIL ATKGYAVTVT GAYDHATRRA VQDLQALHGL PRNGKLSTST
WCTIVGGTVR QSFTHH
//
