ID A0A160DTM1_9GAMM Unreviewed; 781 AA.
AC A0A160DTM1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=I596_1695 {ECO:0000313|EMBL:ANB17719.1};
OS Dokdonella koreensis DS-123.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB17719.1, ECO:0000313|Proteomes:UP000076830};
RN [1] {ECO:0000313|EMBL:ANB17719.1, ECO:0000313|Proteomes:UP000076830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB17719.1,
RC ECO:0000313|Proteomes:UP000076830};
RA Kim J.F., Lee H., Kwak M.-J.;
RT "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC ChEBI:CHEBI:78435; EC=2.4.1.129;
CC Evidence={ECO:0000256|ARBA:ARBA00023988};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004752}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the transpeptidase
CC family. {ECO:0000256|ARBA:ARBA00007090}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 51 family. {ECO:0000256|ARBA:ARBA00007739}.
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DR EMBL; CP015249; ANB17719.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A160DTM1; -.
DR STRING; 1300342.I596_1695; -.
DR KEGG; dko:I596_1695; -.
DR PATRIC; fig|1300342.3.peg.1654; -.
DR OrthoDB; 9766909at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000076830; Chromosome.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR011815; PBP_1c.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR NCBIfam; TIGR02073; PBP_1c; 1.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF15; PENICILLIN-BINDING PROTEIN 1C; 1.
DR Pfam; PF06832; BiPBP_C; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000076830}.
FT DOMAIN 49..225
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 303..523
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 697..777
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 781 AA; 84081 MW; E348AE140E1B9C4D CRC64;
MPLAWRRRLR RGLLLVVLVA AVLAVLDRCF PLPLPDASGA GAIVLARDGQ PLRAFPDRDG
VWRYPVTPEQ VSPLYVEALL TYEDRWFAHH PGVNPLALAR AAGQGLRHRR MVSGGSTLTM
QVARILDGTP HDLGGKLRQI ARALQLELHL SKREILTLYL NHAPFGGTIE GVEAAAWAYL
GKSAQRLSRA EAALLAVLPQ APTRLRPDRN PDVARAYRDK VLDRMARLGV WSAGEVADAR
IETVASRSLQ PPMTAALLAE RLRTARPGER RLASTIDAGL QRALEARVAD YLARLPERTS
AALLVVDNAS LDALAYVGSG AFGSEARLGH VDMVRAWRSP GSTLKPFLYG LALDDGLIHS
ESLLVDAPQA FGGYRPGNFD MAFNGPVSAA QALRLSLNIP AVELLDRLTP ARFAARLEHA
GITLRLPRGA APNLSMILGG AGARLEDLVG AYAAFNRGGV AGRVRYLHDA PAIDRRVLSE
GAAWIVREML EANPRPGYAS GSFDTGSRPR VAWKTGTSYG FRDAWALGTT RQYTVGVWIG
RPDGTPLPGQ YGAITALPLL FQAIDSLPRA SVAPAPQPPP STVSQVEICW PLGLAYDPAQ
PELCHQKHRA WILDGVIPPT LAEREATRWS AGVVRLNVDA ASGHRLGPGC DDRAARPLAI
ARWPVAAYPW LPRETRRRAS LPPLAAGCAD DGLAHLQGLR IDGISDGATL ARAPNSDKPA
RVRLRALGAE GEVLWLVDGL LVGRTQGGQP IEQPFATTGE RTLTALAADG AYAQVRIRVL
R
//
