ID C5BDM8_EDWI9 Unreviewed; 541 AA.
AC C5BDM8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=NT01EI_0406 {ECO:0000313|EMBL:ACR67644.1};
OS Edwardsiella ictaluri (strain 93-146).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Hafniaceae; Edwardsiella.
OX NCBI_TaxID=634503 {ECO:0000313|EMBL:ACR67644.1, ECO:0000313|Proteomes:UP000001485};
RN [1] {ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|Proteomes:UP000001485};
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACR67644.1, ECO:0000313|Proteomes:UP000001485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-146 {ECO:0000313|EMBL:ACR67644.1,
RC ECO:0000313|Proteomes:UP000001485};
RX PubMed=22247535; DOI=10.1128/JB.06522-11;
RA Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA Schuster S.C., Gipson J., Zaitshik J., Landry C., Banes M.M.,
RA Lawrence M.L.;
RT "Genome Sequence of Edwardsiella ictaluri 93-146, a Strain Associated with
RT a Natural Channel Catfish Outbreak of Enteric Septicemia of Catfish.";
RL J. Bacteriol. 194:740-741(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 -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; CP001600; ACR67644.1; -; Genomic_DNA.
DR AlphaFoldDB; C5BDM8; -.
DR STRING; 67780.B6E78_12805; -.
DR KEGG; eic:NT01EI_0406; -.
DR HOGENOM; CLU_014322_2_3_6; -.
DR Proteomes; UP000001485; Chromosome.
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; cd00118; LysM; 2.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01476; LysM; 2.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 2.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..541
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002948614"
FT DOMAIN 436..479
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 495..538
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 128..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 58077 MW; 5DE555446CC265B3 CRC64;
MQRFLRITLP LALGWCLATM AGAAQLTNIQ VSNGERQAVV TLTFNAPPEL SQRVERSPDR
VLVEIANSKR ITGGLPMQFS GENMLSRIRD GGEQRAGKVL LVLDTTARPR VSVTRRGNRA
VLTLRAESRA AVAPAPPPAS AGKNSLHSRP RQAVPAAAPL PSVPVSAVKK SGRYDGSQIV
VAIDAGHGGQ DPGAIGQDGL REKDVTLAIA RRLQGLMDDD PMFQPVLTRG GDYFISVMGR
SDVARRQKAN LLISIHADAA PNRSANGASV WVLSNRRANS EMAGWLEQHE KQSELLGGAG
DVLANSNQDK YLSQTVLDLQ FGHSQRVGYD VAVQVLRQMQ SVVRLHKRDP EHASLGVLRS
PDIPSLLVET GFISNSEGER QLGSGQHQER IARAIYLGVR SYFLAHPLQS GPKVENRPQQ
ASAAGNAAAA ASSASGIHVV KRGETLLGIA NRYGSTLSGM MRLNNLKKEG VWVGQRLKVP
SVGGSAQPAT ASVPRIHLVK RGDTLTRIAA HYGVSMDALR QANKMKSDGV QLGQRLRIPS
R
//
