ID A0A1A5YB01_9BACL Unreviewed; 222 AA.
AC A0A1A5YB01;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=A7K91_15560 {ECO:0000313|EMBL:OBR62806.1};
OS Paenibacillus oryzae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1844972 {ECO:0000313|EMBL:OBR62806.1, ECO:0000313|Proteomes:UP000092024};
RN [1] {ECO:0000313|EMBL:OBR62806.1, ECO:0000313|Proteomes:UP000092024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1DrF-4 {ECO:0000313|EMBL:OBR62806.1,
RC ECO:0000313|Proteomes:UP000092024};
RA Zhang J., Zhang X.;
RT "Paenibacillus oryzae. sp. nov., isolated from the rice root.";
RL Submitted (MAY-2016) 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:OBR62806.1}.
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DR EMBL; LYPA01000078; OBR62806.1; -; Genomic_DNA.
DR RefSeq; WP_068686920.1; NZ_LYPA01000078.1.
DR AlphaFoldDB; A0A1A5YB01; -.
DR STRING; 1844972.A7K91_15560; -.
DR OrthoDB; 9794294at2; -.
DR Proteomes; UP000092024; 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 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 SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 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:UP000092024};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT DOMAIN 13..152
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 222 AA; 24496 MW; BBE20F1116D240E8 CRC64;
MFPYIIDHIP VATPHNRRPG LAIGATSITI HNTANPSSTA RNERNWLTNP SNTATASFHI
VIDQKEAIEC IPLTEIAWHA GDGNTAGSGN RTSIGIEICE SGNYDVTLRN AAELVAGMLQ
QRGWDTDRLR RHYDWSGKNC PRLMNSDGQW KGWLDFVGMV KEKLDGSGEE GGGEKVLKPE
DANNIIRFLS AAYMATDSPD ARKEFNRLAN ELRRVSGQPP QP
//
