ID A0A1T5H1D1_9BACI Unreviewed; 237 AA.
AC A0A1T5H1D1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, 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};
DE AltName: Full=Autolysin {ECO:0000256|ARBA:ARBA00032390};
DE AltName: Full=Cell wall hydrolase {ECO:0000256|ARBA:ARBA00030881};
GN ORFNames=SAMN06295926_12835 {ECO:0000313|EMBL:SKC14486.1};
OS Lysinibacillus sp. AC-3.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1680467 {ECO:0000313|EMBL:SKC14486.1, ECO:0000313|Proteomes:UP000190941};
RN [1] {ECO:0000313|EMBL:SKC14486.1, ECO:0000313|Proteomes:UP000190941}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC-3 {ECO:0000313|EMBL:SKC14486.1,
RC ECO:0000313|Proteomes:UP000190941};
RA Peterson S.W.;
RL Submitted (FEB-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}.
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DR EMBL; FUYW01000028; SKC14486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5H1D1; -.
DR STRING; 1680467.SAMN06295926_12835; -.
DR Proteomes; UP000190941; 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 Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT DOMAIN 15..164
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 237 AA; 27037 MW; C76B499B01F50134 CRC64;
MTYTFRQILL PPTKYPIKAP YIMFPQFITV HNTANDAPAA NEIAYMLSNN NQVSYHVAVD
DKEVIQAIPF NRNAWHCGDG GGSTDPNALT KGNRLSIGVE ICYSKSGGAC YVAAEENAVQ
YIAKLLKQYG WGVDRVKKHQ DWNGKYCPHR ILSEERWNSF LNRIEEAMKP KETEKDDDKM
QFTNETTKAA VRDYIKQAVD KKLIEKSWLD KFDNGTMTTG DYEGLKLIIA QRENNKK
//