ID A0A158I048_9BURK Unreviewed; 507 AA.
AC A0A158I048;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=AWB66_02837 {ECO:0000313|EMBL:SAL49938.1};
OS Caballeronia telluris.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=326475 {ECO:0000313|EMBL:SAL49938.1, ECO:0000313|Proteomes:UP000054717};
RN [1] {ECO:0000313|EMBL:SAL49938.1, ECO:0000313|Proteomes:UP000054717}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22936 {ECO:0000313|EMBL:SAL49938.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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; FCNZ02000009; SAL49938.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158I048; -.
DR STRING; 326475.AWB66_02837; -.
DR Proteomes; UP000054717; 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; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000054717}.
FT DOMAIN 337..492
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 174..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 507 AA; 55302 MW; 3E3E0BA529184BD4 CRC64;
MSRKMLIKPF RSIESTATAS HNWKRRQVLR AGVSTIALAL VAPRLAHASS VLGVRVWPAR
DYTRVTIESD QPLANNQQLL QGPDRLVVDL NGLDLDQELK DLVSKITPND PQIQAVRIGQ
YQPHVVRMVF DLKGSVKPQV FTLTPIGSYK YRLVFDLYPA VAPDPLMELL AQSEHKQEAF
DKSNPNPAPP PATLSGPTQP QRSPAPDNPD DFFQKYADNT DPPRPAAPVV PAPRPSVKPA
VPLAPPVATK NDSDDDTYAF STPKQKSKSA TTRLLTVAID PGHGGEDPGA IGGGGTYEKH
IALDIAKKLR AKIDAQPNMR AMMTRDADFF VPLNVRVQKA RRVEADLFVS IHADAFTSPE
ARGSSVFALS DHGASSAAAR WLANKENESD SVGGINVRSQ DVSVNRALFD MSTTAQIRDS
MRYGNFVLNE IGGINKLHKG SVEQAGFAVL KAPDIPSILV ETAFISNPDE EARLNDDAYR
EKMANAILKG IKRYFAANPP LAKSRMT
//
