ID A0A124IHE6_9FIRM Unreviewed; 194 AA.
AC A0A124IHE6;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=APF76_14960 {ECO:0000313|EMBL:KUO53089.1};
OS Desulfitibacter sp. BRH_c19.
OC Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC Desulfitibacter.
OX NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO53089.1, ECO:0000313|Proteomes:UP000053015};
RN [1] {ECO:0000313|EMBL:KUO53089.1, ECO:0000313|Proteomes:UP000053015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO53089.1};
RA Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT "Microbial metabolic network in the subsurface.";
RL Submitted (OCT-2015) 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 -!- 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:KUO53089.1}.
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DR EMBL; LOER01000007; KUO53089.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124IHE6; -.
DR STRING; 1734395.APF76_14960; -.
DR Proteomes; UP000053015; 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; 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; 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 2..115
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
SQ SEQUENCE 194 AA; 22071 MW; D13CE2E2F1509542 CRC64;
MCPREFIVLH HTGAEETDAE HVKRNHLQKG FRDIGYNYII ENNGKVITGR PLDIPGAHCI
GDRMNFRSIG VALIGNFEER SPYAEQINSL IPLLQGLQLK HSIKLENILL HKLVKGSSTK
CPGKLFNWNE IKLALYPDVP WMWQVKVGTY FDKNIALNTV TALRDMGFPA LIERINIEDQ
VKTVLTTNKC SIYN
//
