ID C5S4P6_9PAST Unreviewed; 182 AA.
AC C5S4P6;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=AM305_00925 {ECO:0000313|EMBL:EER46135.1};
OS Actinobacillus minor NM305.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=637911 {ECO:0000313|EMBL:EER46135.1, ECO:0000313|Proteomes:UP000005532};
RN [1] {ECO:0000313|EMBL:EER46135.1, ECO:0000313|Proteomes:UP000005532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM305 {ECO:0000313|EMBL:EER46135.1,
RC ECO:0000313|Proteomes:UP000005532};
RX PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA Arya G., Niven D.F.;
RT "Production of haemolysins by strains of the Actinobacillus
RT minor/"porcitonsillarum" complex.";
RL Vet. Microbiol. 141:332-341(2010).
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:EER46135.1}.
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DR EMBL; ACQL01000153; EER46135.1; -; Genomic_DNA.
DR RefSeq; WP_005825926.1; NZ_ACQL01000153.1.
DR AlphaFoldDB; C5S4P6; -.
DR eggNOG; COG3023; Bacteria.
DR OrthoDB; 8754850at2; -.
DR Proteomes; UP000005532; 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 InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
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.
DR PROSITE; PS00018; EF_HAND_1; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..149
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT DOMAIN 3..141
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
SQ SEQUENCE 182 AA; 20273 MW; CCCC887453D76E13 CRC64;
MSLPITKIVV HCSATTNGKS LAQQGKSSAQ IIDSWHKARG FRRSANAVRH FNSHLSHIGY
HFVIDVDGTV ETGRQVGEIG AHVRGHNTHS VGICLVGGVG EGKEKSYARF TTAQWHALEL
LLRQLEANHP RAKVYGHRDL SPDIDGDGSI TPNEWVKTCP NFDVWEWLDR GETVFVEHLF
KE
//
