ID A0A171KX95_9BURK Unreviewed; 759 AA.
AC A0A171KX95;
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=AAV32_03575 {ECO:0000313|EMBL:KKO73512.1};
OS Kerstersia gyiorum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Kerstersia.
OX NCBI_TaxID=206506 {ECO:0000313|EMBL:KKO73512.1, ECO:0000313|Proteomes:UP000078084};
RN [1] {ECO:0000313|EMBL:KKO73512.1, ECO:0000313|Proteomes:UP000078084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CG1 {ECO:0000313|EMBL:KKO73512.1,
RC ECO:0000313|Proteomes:UP000078084};
RA Greninger A.L., Kozyreva V., Chaturvedi V.;
RT "Genome sequence of Kerstersia gyiorum CG1.";
RL Submitted (APR-2015) 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}.
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:KKO73512.1}.
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DR EMBL; LBNE01000001; KKO73512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A171KX95; -.
DR STRING; 206506.AAV32_03575; -.
DR PATRIC; fig|206506.3.peg.783; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000078084; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000078084}.
FT DOMAIN 45..209
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 286..528
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 672..755
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 759 AA; 82642 MW; E6F8517B50CE852F CRC64;
MLVAVALLWL ADRCFPLPMP AAATARVVLA EDGTPLWRFA DADGVWRYEA RREDISPYYI
EALLAYEDRW FWQHPGINPV ALGRATWLNL RYGRVVSGGS TISMQVARLL DPHPRTVAGK
LRQVWRTLQL EWHYSKEEIL ELYLNRAPFG GVLEGVAAAS WTYLGKSPAE LSRAEAALLA
VLPQAPSRLR PDRHPELAQQ ARDKVLARMA EQGIWSAAEV EEALMEPVHL FTLPRPQAAP
LLARRLVQQQ GAAPVIRTTI DGMLQLRIEQ AMQRWKATLP PRVSAAVLVI EHDTMAVRAY
AGSVDFLDTA RNGQVDMVTA IRSPGSTLKP FLFSLALDEG LIHSSSLLQD VPRHYGEYRP
QNFAADFSGP VSAAEALSRS LNLPLVQLLE AYGPVRFATE LREAGLPLRL PQQAVPNLSL
ILGGAGTSLE QLVAAYSVYA RGGNMAAPRY ADDEPLLERR LISPGAAWIT RQVLSGRLTP
DQPAAGANAL AWKTGTSYGF RDAWAVGVGP RYLIGVWVGR PDGAPVAGQF GQAAAAPLLF
QIHRLAHRES ASLARQMAAG APAQVGTARI CWPLGQPMPE GSPDCRQARQ AWVLDGVTPP
TLLAGDQRPG AGLLLDYWVS AAGLRVAAAC PGARPASMVA WPQPLEPWLP RQERLSARLP
GVDPACPPPV VDTGTPLVIL GVREGDRLRR PARSQAPVTL NLSALGGSGQ RWWYMNGWAL
QERELAGLLK VALRQPGRYR ITLLDEAGQT ASVGFEVLE
//
