ID A0A1Y5K2L1_9BACL Unreviewed; 501 AA.
AC A0A1Y5K2L1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, 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};
GN ORFNames=B1748_29215 {ECO:0000313|EMBL:OUS70317.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS70317.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS70317.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS70317.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-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 -!- 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:OUS70317.1}.
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DR EMBL; MXQD01000049; OUS70317.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5K2L1; -.
DR OrthoDB; 9794294at2; -.
DR Proteomes; UP000195591; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
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; IPR018711; NAGPA.
DR InterPro; IPR001119; SLH_dom.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF11; N-ACETYLMURAMOYL-L-ALANINE AMIDASE XLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF09992; NAGPA; 1.
DR Pfam; PF00395; SLH; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51272; SLH; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Competence {ECO:0000256|ARBA:ARBA00023287};
KW Reference proteome {ECO:0000313|Proteomes:UP000195591};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT DOMAIN 446..501
FT /note="SLH"
FT /evidence="ECO:0000259|PROSITE:PS51272"
SQ SEQUENCE 501 AA; 54740 MW; 773ABFFD2CA58E66 CRC64;
MIAHKRIRIA SGKVEEGPLT YTLSGQYSKG EGWTDMRAVD VPTASIQRVE LVTGKGKTIS
SILADLVKQH GGNWICFNAS YFNPNDGALL GLTYRDGKAI YPDVKGKTEQ RPHLYYKGGK
WGIGRQDKPD GHTLAVSAVP TLSAGGKAID PPRTAEVTPS DVLGTNPRMI AGIKADGTLG
LILVDGRGTY DKGLTSKEAG IMAVHYGYPE SVNLDGGWSA ELATNNRQML DALEIDKVNK
KRQYHVADMS QDYNERVVHH AIAIQIDPEK LFPTYIVDHI PTNTPNNRRP GHRLMPTTIT
IHNTANPSST ARNERSWLTN PANTATASYH IVLDDKETVE TLPLNESAWH AGDGSGAASG
NRTSIGIEIC ESGNYAVTLS RAVELVAKML KERGWGVDRL RRHYDWSGKI CPRLMYDGGS
WAGWIDFKAR VAAAINPPIV KPEPEQPVKP VDDITGHWAE SALRDAIKDG ALAGFPDGTI
RPDEPLTRAQ YAVIRSRERQ G
//
