ID D8MM96_ERWBE Unreviewed; 551 AA.
AC D8MM96;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiB {ECO:0000313|EMBL:CAX57980.1};
GN OrderedLocusNames=EbC_04490 {ECO:0000313|EMBL:CAX57980.1};
OS Erwinia billingiae (strain Eb661).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=634500 {ECO:0000313|Proteomes:UP000008793};
RN [1] {ECO:0000313|EMBL:CAX57980.1, ECO:0000313|Proteomes:UP000008793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eb661 {ECO:0000313|EMBL:CAX57980.1,
RC ECO:0000313|Proteomes:UP000008793};
RX PubMed=20565991; DOI=10.1186/1471-2164-11-393;
RA Kube M., Migdoll A.M., Gehring I., Heitmann K., Mayer Y., Kuhl H.,
RA Knaust F., Geider K., Reinhardt R.;
RT "Genome comparison of the epiphytic bacteria Erwinia billingiae and E.
RT tasmaniensis with the pear pathogen E. pyrifoliae.";
RL BMC Genomics 11:393-393(2010).
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; FP236843; CAX57980.1; -; Genomic_DNA.
DR AlphaFoldDB; D8MM96; -.
DR STRING; 634500.EbC_04490; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR KEGG; ebi:EbC_04490; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_014322_2_3_6; -.
DR Proteomes; UP000008793; 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; IPR021731; AMIN_dom.
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; PF11741; AMIN; 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 Hydrolase {ECO:0000313|EMBL:CAX57980.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008793};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..551
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003117931"
FT DOMAIN 446..489
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 505..548
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 130..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 58835 MW; 88D7A4E21F4DE39A CRC64;
MKFGLVLALL LTTFSSLAAN LSDIKVSNGD DKATVTLSFN GQPVYGFFPL HNPDRVVLDI
RQSGVIKGLP LTFSGENIVK RIRSSTPKDK QSIRLVFELT QASKTRAVTQ REGNNYNVVF
TIAGTRPAAT ASRRPAEVSS ASSSAPSAPV ENPFKGNPVT AVSSGNDVVR PGRTPVSANE
AVIVAIDAGH GGQDPGAIGA GGLKEKNVTI AIARKLKALL NADPMFKGVM TRDGDYFISV
MGRSDVARKQ NANVLVSIHA DAAPNRSASG ASVWVLSNRR ANSEMAGWLE QHEKQSELLG
GAGDLLANSQ ADPYLSQAVL DLQFGHSQRV GYDVAVKVIA QLQRVGSLHK RRPEHASLGV
LRSPDIPSLL VETGFISNPS EERLLGSSAY QQKIAESIYK GLRNYFLAHP LQSIPKEENR
PLQSAATVNV EPNPAPDTTQ YTGAIQRHVV KRGETASGIA ARYGISMATL RSMNTLKKDV
VWVGQRLKVP AGSQPAAVTK AKTPVRHKVV RGDSLTAIAA HYGVSPKAIQ QANKMKSQNV
MLGQTLTIPT S
//