ID A0A2W0HVU7_9BACI Unreviewed; 293 AA.
AC A0A2W0HVU7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE AltName: Full=Autolysin {ECO:0000256|ARBA:ARBA00032390};
DE AltName: Full=Cell wall hydrolase {ECO:0000256|ARBA:ARBA00030881};
GN ORFNames=CR205_04275 {ECO:0000313|EMBL:PYZ97818.1};
OS Alteribacter lacisalsi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alteribacter.
OX NCBI_TaxID=2045244 {ECO:0000313|EMBL:PYZ97818.1, ECO:0000313|Proteomes:UP000248066};
RN [1] {ECO:0000313|EMBL:PYZ97818.1, ECO:0000313|Proteomes:UP000248066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YSP-3 {ECO:0000313|EMBL:PYZ97818.1,
RC ECO:0000313|Proteomes:UP000248066};
RA Wang H.;
RT "Bacillus sp. nov., a halophilic bacterium isolated from a Yangshapao
RT Lake.";
RL Submitted (OCT-2017) 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:PYZ97818.1}.
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DR EMBL; PDOF01000001; PYZ97818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2W0HVU7; -.
DR OrthoDB; 9812621at2; -.
DR Proteomes; UP000248066; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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 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.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000248066};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..136
FT /note="Peptidoglycan recognition protein family"
FT /evidence="ECO:0000259|SMART:SM00701"
FT DOMAIN 15..144
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 293 AA; 31733 MW; CBD1425CBB5A3AC6 CRC64;
MKIIDLTGNL PRHQTKRYRK RLVRTITDIT IHHSGTERGS AHSFASYHVN KNGWPGIGYH
FVIEQDGAII KTNTLSTVSY HAGQVNAVSA GICLTGNFSS HGPGTEQWDA LVFLTKKLLH
ELGLSPDQVQ GHCEQPGAST VCPGFSTESL RRCLMGSPVL KRGDRGAGVV RLQKKLMASG
VNSGPVDGLF GVLTETALRH FQKVRRLRVD GIYGAETNEA LSASRRVLQR LSPMMKGIDV
ILVQMTAGAV PDSLFGPATQ ASVRAYQKTK KIASDGIVGP VTWRMILNGK ALP
//
