ID A0A085ZDI5_9FLAO Unreviewed; 301 AA.
AC A0A085ZDI5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=IW19_24740 {ECO:0000313|EMBL:KFF02499.1};
OS Flavobacterium reichenbachii.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=362418 {ECO:0000313|EMBL:KFF02499.1, ECO:0000313|Proteomes:UP000028715};
RN [1] {ECO:0000313|EMBL:KFF02499.1, ECO:0000313|Proteomes:UP000028715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25512 {ECO:0000313|EMBL:KFF02499.1,
RC ECO:0000313|Proteomes:UP000028715};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Flavobacterium reichenbachii LMG 25512.";
RL Submitted (JUL-2014) 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 -!- 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:KFF02499.1}.
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DR EMBL; JPRL01000005; KFF02499.1; -; Genomic_DNA.
DR RefSeq; WP_035690319.1; NZ_MUHF01000017.1.
DR AlphaFoldDB; A0A085ZDI5; -.
DR STRING; 362418.IW19_24740; -.
DR eggNOG; COG3023; Bacteria.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000028715; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
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;
FT DOMAIN 89..220
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 301 AA; 33674 MW; 8D882AB8FC0C30FA CRC64;
MAKKHFCYLI LAIIMASCST NPYKTTEKAY DQQLKTLENQ ITSKEAQQIP SVSPLAIDTT
YAQQLGIVKD SISKTGSTSL LNGISTEWIG TVNFNLRKPS FIIIHHTAQD SIQQTINTFT
KTRTQVSSHY IISENGKVVQ MLNDYLRAWH AGNSTWGKNT DLNSSSIGIE LDNNGFKPFT
EAQISSLVAL LTKLKKDYNI PTQNILGHAD IAPGRKQDPS ALFPWKTLAE KGFGIWPDAV
LEEAPFDFKI EPALRIIGYN TKNLAAAIQA FKLHYIQTDN TSVLDRKTID TIYSIYKKQI
Q
//