ID B2JDT5_PARP8 Unreviewed; 515 AA.
AC B2JDT5;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
DE Flags: Precursor;
GN OrderedLocusNames=Bphy_0519 {ECO:0000313|EMBL:ACC69711.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC69711.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC69711.1; -; Genomic_DNA.
DR RefSeq; WP_012399936.1; NZ_CADFGH010000001.1.
DR AlphaFoldDB; B2JDT5; -.
DR STRING; 391038.Bphy_0519; -.
DR KEGG; bph:Bphy_0519; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_2_4; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000001192; Chromosome 1.
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 Hydrolase {ECO:0000313|EMBL:ACC69711.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001192}.
FT DOMAIN 345..500
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 175..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..247
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 515 AA; 55715 MW; 25777BF52F137244 CRC64;
MSRKMLIKPF RSIESAATAT HNWRRRQILH AGASTLVLGL AAPRLALASS VLGVRVWPAR
DYTRVTIESD QPLQNTQQLL QGPDRLVVDL NGLDLDQALK DLVSKIAPND PQIQSVRVGQ
YQPHVVRMVF DLKGSVKPQV FTLPPVGAYK YRLVFDLYPA VAPDPLMDLL AQTERKEQQL
KDNAAPPAAT LNGPTTPPGD NSDAFFEKYA QNNAPSPAAP VPHPPLHGAP APTPHMPPKP
APTPAPPVIA RNNDSDADNA GDNNDDEYKF TAPKKGSNTV RLLTVAIDPG HGGEDPGAIG
GSGTYEKHVA LDIAKKLRAK IDAQPNMRAM MTRDADFFVP LNVRVQKARR VGADLFVSIH
ADAFTTPEAS GSSVFALSEH GASSAAARWM ANKENSSDQI GGINIKSADA SVNRALFDMS
TTAQIRDSMR YGTFVLKEIG GINRLHKGSV EQAGFAVLKA PDIPSILVET AFISNPDEER
RLNDDAYRDK MANAIMSGIK RYFAANPPLA KSRMT
//
