ID A0A1I0E256_9BACI Unreviewed; 230 AA.
AC A0A1I0E256;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
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=SAMN05216389_11056 {ECO:0000313|EMBL:SET38685.1};
OS Oceanobacillus limi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=930131 {ECO:0000313|EMBL:SET38685.1, ECO:0000313|Proteomes:UP000198618};
RN [1] {ECO:0000313|EMBL:SET38685.1, ECO:0000313|Proteomes:UP000198618}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBRC-M 10780 {ECO:0000313|EMBL:SET38685.1,
RC ECO:0000313|Proteomes:UP000198618};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; FOHE01000010; SET38685.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0E256; -.
DR STRING; 930131.SAMN05216389_11056; -.
DR OrthoDB; 66275at2; -.
DR Proteomes; UP000198618; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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 PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198618};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 54..220
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 230 AA; 26521 MW; C54C2237171CE1BE CRC64;
MKRNVFYLIL CCVGIVAFLF IHHLRSESSS ITVKDVEESQ QEERFKAEVN EILLPLENSE
FRLEPVTHVV IHYMSNAVEK PHDPYKLEDI YSIFLASGLS SHYVIDRKGN IYQLVAEERI
AYHAGAGRLT TVPNYEDKLN DYSIGIELLA IGTKDEMKPL IDEQTYEVIP SQSIGFTEDQ
YQSLKELLDD IQVRHPDVHL NRDHIVGHDE YAPKRKNDPG SLFDWDKLGF
//
