ID J2SNI9_FLASC Unreviewed; 301 AA.
AC J2SNI9;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=PMI10_00205 {ECO:0000313|EMBL:EJL67042.1};
OS Flavobacterium sp. (strain CF136).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1144313 {ECO:0000313|EMBL:EJL67042.1, ECO:0000313|Proteomes:UP000007287};
RN [1] {ECO:0000313|EMBL:EJL67042.1, ECO:0000313|Proteomes:UP000007287}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF136 {ECO:0000313|EMBL:EJL67042.1,
RC ECO:0000313|Proteomes:UP000007287};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL67042.1}.
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DR EMBL; AKJZ01000006; EJL67042.1; -; Genomic_DNA.
DR RefSeq; WP_007803471.1; NZ_AKJZ01000006.1.
DR AlphaFoldDB; J2SNI9; -.
DR STRING; 1144313.PMI10_00205; -.
DR PATRIC; fig|1144313.4.peg.198; -.
DR eggNOG; COG3023; Bacteria.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000007287; 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;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..301
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003754682"
FT DOMAIN 89..220
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 301 AA; 33713 MW; D3E3E8C0EBCFE552 CRC64;
MLKKHLCYLI LAISIISCAT KNPYKDTEKV YDKQLKTLEN QIASKEVQQI PSNPVVIDTS
YAQQLGIVKD TLSKTGSTAL LNGINTEWIG TVNFNLRKPS FIIIHHTAQD SIQQTINTFI
KTKTQVSAHY VISENGKVVQ MLNDYLRAWH AGASTWGKNT DLNSSSIGIE LDNNGSKPFT
EAQISSLVAL LTKLKKDYNI PTQNIIGHSD IAPGRKQDPS ALFPWKTLAE KGFGIWPDEI
LEEAPFDFKI EPALRIIGYN TKNLSAAIIA FKLHYIQTDT SVTLDRKTID TIYSIYKKQL
Q
//
