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Database: UniProt
Entry: A0A1B3PP63_9BURK
LinkDB: A0A1B3PP63_9BURK
Original site: A0A1B3PP63_9BURK 
ID   A0A1B3PP63_9BURK        Unreviewed;       481 AA.
AC   A0A1B3PP63;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE            EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN   ORFNames=BSY15_2730 {ECO:0000313|EMBL:AOG24560.1};
OS   Acidovorax sp. RAC01.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1842533 {ECO:0000313|EMBL:AOG24560.1, ECO:0000313|Proteomes:UP000094760};
RN   [1] {ECO:0000313|Proteomes:UP000094760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC01 {ECO:0000313|Proteomes:UP000094760};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-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; CP016447; AOG24560.1; -; Genomic_DNA.
DR   RefSeq; WP_069105235.1; NZ_CP016447.1.
DR   AlphaFoldDB; A0A1B3PP63; -.
DR   STRING; 1842533.BSY15_2730; -.
DR   KEGG; acra:BSY15_2730; -.
DR   PATRIC; fig|1842533.3.peg.2836; -.
DR   OrthoDB; 9806267at2; -.
DR   Proteomes; UP000094760; 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; 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:UP000094760}.
FT   DOMAIN          311..466
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000259|SMART:SM00646"
FT   REGION          162..237
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   481 AA;  50730 MW;  915C22C03CA9235B CRC64;
     MTGLPPSPSR RALLQTGSLV LLLGTQQIAR GATILAVRVW PAPEYSRVTI ESDGALVAKQ
     FFVTSPPRLA VDIEGIDLSP ELRELVAKVK PDDPNIAGIR VGQNAPGVVR LVVDLKQPAM
     PQVFTLPPVA AYRHRLVFDL YPADPVDPLE ALIAERLRDA GGPAPAAGRT APPAPAVTAH
     TTSPAAPATP ATADPLGDLI AQRTQRPGTG ETSAPTVAAA PAAADAAGKR AGANQPTATR
     TDRIIIVALD PGHGGEDPGA IGPAGTREKD VVLRVAYLLR DRINATTVGG NPMRAYLTRD
     GDFFVPLGVR VQKAQRVQAD LFISIHADAF TVPTARGASV FALSQGGASS TAARWLANKE
     NQADLVGGIN VKSRDQHVQR ALLDMSTTAQ INDSLKLGSA LLGEIGTVGR LHKPRVEQAG
     FAVLKAPDIP SVLVETAFIS NPEEEQRLRS SAYQERLADA LMRGITRYFA RNPPLARSRS
     V
//
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