ID D4VNC0_9BACE Unreviewed; 797 AA.
AC D4VNC0;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BN890_44360 {ECO:0000313|EMBL:CDM06818.1};
OS Bacteroides xylanisolvens SD CC 1b.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=702447 {ECO:0000313|EMBL:CDM06818.1, ECO:0000313|Proteomes:UP000019380};
RN [1] {ECO:0000313|EMBL:CDM06818.1, ECO:0000313|Proteomes:UP000019380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ramaraj T., Sundararajan A., Mudge J., Schilkey F.D., Delvecchio V.,
RA Donlon M., Ziemer C.;
RT "Improved hybrid genome assemblies of Bacteroides xylanisolvens SD CC 1b
RT and Bacteroides xylanisolvens SD CC 2a using Illumina and 454 Sequencing.";
RL Submitted (DEC-2013) 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 -!- 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:CDM06818.1}.
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DR EMBL; CBXG010000049; CDM06818.1; -; Genomic_DNA.
DR AlphaFoldDB; D4VNC0; -.
DR Proteomes; UP000019380; 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:0009252; P:peptidoglycan biosynthetic process; IEA:InterPro.
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 4: Predicted;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW Glycosyltransferase {ECO:0000313|EMBL:CDM06818.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transferase {ECO:0000313|EMBL:CDM06818.1}.
FT DOMAIN 51..209
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 287..573
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 705..793
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
FT REGION 464..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 797 AA; 89313 MW; D652A18F3937DD66 CRC64;
MTISITLLII GYIFCLPRQL FHVPYSTVVT DRNEELLGAR IASDGQWRFP PRKTTPEKIK
QCLITFEDKH FYHHWGVNPL ATGRALYQNL KNKRVVSGGS TLTMQTIRLA RNKPRTLGEK
VVEMIWATRL EFRASKEEIL SMYVSHAPFG GNVVGLDAAA WRYFGHSAED LSWAESAMLA
VLPNAPAMIH LSKGRKTLLS KRNRLLKQLL EEEIIDASTY ELAVSEPLPD EPHPLPQIAP
HLVSRFYQER NGLYTRSTID RGIQSHIESL AERWSNEFNR SDIRNLAILV IDIPTNQVVA
YCGNVHFDRK QGGSQVDVIQ APRSTGSILK PFLYNAMLQE GSLLPKMLLP DVPVNINGFT
PQNFSMQFEG AVPASEALAR SLNIPAVTML QRYGVPKFHH LLQQMEFKTI NRTASHYGLS
LILGGAEATL WDVTNAYAQM GRSLSSSPSP TVSQGKEAQI LLETENTEQI NNDTKQTSRN
HKSNHNKQEK REQSNSSPLS VEEDSEETTS AKTGAAWLTL SALTEVNRPE EIDWKSIPSM
QTIAWKTGTS YGFRDAWAVG VTPRYTVGVW VGNATGEGKP GLVGAQTAGP VLFDIFSYLP
SSPWFERPTG VFVDAEICRQ SGHLKGRFCE ETDTVLILPA GLRTEACPYH HLVTLSADES
HRIYENCANT EPTIQKSWFA LPPVWEWYYK QHHPEYKPLP PFKAGCGEDS FQSMQFIYPP
MNAHIKLPKQ LDGSKGFLTV ELAHSNPNAT IFWHLDDTYQ TQTQDFHKIS LQPAPGKHSL
TAVDGEGNTV STTFFIE
//
