ID J2KYQ1_9BURK Unreviewed; 750 AA.
AC J2KYQ1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=PMI12_01379 {ECO:0000313|EMBL:EJL78118.1};
OS Variovorax sp. CF313.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1144315 {ECO:0000313|EMBL:EJL78118.1, ECO:0000313|Proteomes:UP000007277};
RN [1] {ECO:0000313|EMBL:EJL78118.1, ECO:0000313|Proteomes:UP000007277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF313 {ECO:0000313|EMBL:EJL78118.1,
RC ECO:0000313|Proteomes:UP000007277};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EJL78118.1}.
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DR EMBL; AKIW01000020; EJL78118.1; -; Genomic_DNA.
DR RefSeq; WP_007830419.1; NZ_AKIW01000020.1.
DR AlphaFoldDB; J2KYQ1; -.
DR PATRIC; fig|1144315.3.peg.1372; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000007277; Unassembled WGS sequence.
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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; 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 Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..750
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003750898"
FT DOMAIN 55..229
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 329..576
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 658..732
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 750 AA; 81473 MW; 91F7A4EDC308E719 CRC64;
MQSAPLFVPA RKALAAALLA AACVHPAWAL VSFEEVKRDF RSSDTEVLDR NGELLQRVRT
DPTVRRGRWT ALADVSPALR TAMVLSEDKR FYEHSGIDWR AVSAAAWANV WNTRTRGAST
ITMQLSGLLD DDLRRASGGR SFTQKIGQTV AAAQLERNWR KDQILEAYLN TVPFRGEIVG
IDALSRTLFG KAPSGLDARE AAVASALVRA PNAKPAAVAQ RACEVLRAME PQQKVDCEAL
DMFTSAAVQR RAFETNEGIA PHAARRVLRE IRDANAVAAP TPALHQRGRE KDSKETGVRT
TLRAPLQRFA LGTLQRHLRE LRERHVEDGA LVVLDNATGE VLAWVGSSGP LSQAAEVDGV
TALRQPGSTL KPLLYGQAIA ERRITAASLI EDSSAQISTA SGLYIPQNYD RRFKGPVSAR
TALAASLNVP AVRTLVMVSP EAFARELRAA GLPLRESGDY YGYSLALGSA EVSLLSLTNA
YRMLANGGRY GTTTLTMRPP VPAERSKPPM LDPRAAFIVG DILSDPNART RTFGLDSILS
TRFWTAVKTG TSKDMRDNWA VGWSQRYTVG VWVGNASGES MWDVSGTSGA APVWAEVMRF
LHAREPSRAP APPPGLVEAR VSFGNGADGN PLEAARSEWF LQGTEQTLFA LDAGMATDAA
SARITAPADG TIIALDPDIP PQRQRVRFDS EGRGVQWRID GKPFERGNSV QWFPWPGRHV
IELVDAGGKV VDQRRLEVRG AGVVTKSARR
//
