ID A0A110B0B4_9SPHI Unreviewed; 279 AA.
AC A0A110B0B4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiD {ECO:0000313|EMBL:BAU52347.1};
GN ORFNames=FHS11_004324 {ECO:0000313|EMBL:MBB3057881.1}, MgSA37_00502
GN {ECO:0000313|EMBL:BAU52347.1};
OS Mucilaginibacter gotjawali.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1550579 {ECO:0000313|EMBL:BAU52347.1, ECO:0000313|Proteomes:UP000218263};
RN [1] {ECO:0000313|EMBL:BAU52347.1, ECO:0000313|Proteomes:UP000218263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA3-7 {ECO:0000313|EMBL:BAU52347.1,
RC ECO:0000313|Proteomes:UP000218263};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Mucilaginibacter gotjawali.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3057881.1, ECO:0000313|Proteomes:UP000539265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8628 {ECO:0000313|EMBL:MBB3057881.1,
RC ECO:0000313|Proteomes:UP000539265};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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};
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DR EMBL; AP017313; BAU52347.1; -; Genomic_DNA.
DR EMBL; JACHWX010000016; MBB3057881.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A110B0B4; -.
DR KEGG; mgot:MgSA37_00502; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000218263; Chromosome.
DR Proteomes; UP000539265; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
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:SF10; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:BAU52347.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000218263};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..279
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033728630"
FT DOMAIN 59..195
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 279 AA; 30976 MW; 09D678E3D02B712E CRC64;
MKNGYCYFTL LVLFILASCS PKGPYAVTNK VYKEKTKGYL ATIQMQNPDT LRDSSGMPVP
SAWVGTVNFG IRKPNYVIIH FTAQDSLAQT LHTFTITSTQ VSSHYVIGKD GKVVHMVNDY
LRANHAGLGK WGSVTDMNSC SIGIEIDNNG SEPFTAPQIN SLLLLLAQLK KSYNIPQANF
IGHQDFAPKR KPDPGPYFPW KTLAAHGFGY WSDDVLELAP DGFDYSIALK LIGYDTSDPK
AAVVAFKRHF VQTDIKPEVT QLDLNVLYNV YQKYSPPAP
//
