ID A0A244EBF4_9BURK Unreviewed; 1000 AA.
AC A0A244EBF4;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=A8M77_14750 {ECO:0000313|EMBL:OUM01811.1};
OS Variovorax sp. JS1663.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1851577 {ECO:0000313|EMBL:OUM01811.1, ECO:0000313|Proteomes:UP000195166};
RN [1] {ECO:0000313|EMBL:OUM01811.1, ECO:0000313|Proteomes:UP000195166}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1663 {ECO:0000313|EMBL:OUM01811.1};
RX PubMed=28526789;
RA Mahan K.M., Zheng H., Fida T.T., Parry R.J., Graham D.E., Spain J.C.;
RT "A novel, iron-dependent enzyme that catalyzes the initial step in the
RT biodegradation of N-nitroglycine by Variovorax sp. strain JS1663.";
RL Appl. Environ. Microbiol. 83:0-0(2017).
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 -!- 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:OUM01811.1}.
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DR EMBL; LYMK01000015; OUM01811.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A244EBF4; -.
DR OrthoDB; 8552189at2; -.
DR Proteomes; UP000195166; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
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; 2.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR001264; Glyco_trans_51.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR036950; PBP_transglycosylase.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF33; PEPTIDOGLYCAN GLYCOSYLTRANSFERASE; 1.
DR Pfam; PF00912; Transgly; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
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:ARBA00022670};
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:UP000195166};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:OUM01811.1}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1000
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013235784"
FT DOMAIN 129..285
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
SQ SEQUENCE 1000 AA; 111021 MW; F306ED4095CB7727 CRC64;
MARFRTLLWL GAALAATGAL VAFAVDELRT ARLQSAFWRD VGRDAHFSVA AGPSDALRFP
HSGPYDERLG YKRMPEFIER LEARGYQVTE QARMSPRLMA LYDHGLYGPW REKNQAGLTV
RDCRARTLSQ TRVPQRVYER FEEVPPLLVD ALLFVEDRHL LDAEPAQRNP ALDPERFAKA
GIEQLQRALG ASRSASGGST LATQIEKYRH SPHGRTGSIG DKLRQMASAS LRAYQDGEDT
QVRRRQIVVD YLDTVPLAAR PGYGEVHGLG DGLWAWYGRD FGEVNRLLAD NAEGAPPTEQ
ALERQAEAFK QALSLMIAQR RPSQHLLDNG ESLGRLTDSY LRLMADAGVI APSLRDAALK
ITLKRPSELP PAPRPDFVRR KALNALRGEM TSLLDVPRAY DLERLDLEVD GSLHDQAQAI
AARALMQLRT PAAAKAAGLY GHHLLDPGDD PRRLTYSFTL YERGQDRNLL RVQADSIDQP
FDVNRGARLD LGSTAKLRTL VSYLELVAEL HGRWAEAGTA AVAAWKPNER DPLGQWARHQ
LLNARDRSLP AMLEAAMQRR YSAGEGEAFF TGGGLHSFSN FDRTHGGPMT VQEAFRHSVN
LVFIRLMRDI VRHRMYGDGA AGRRLLEDPA DPSRREMLVL FADREGSAFL ARFHRKYKGK
TPAEAEALLL KGLRPTAPRL ASVLFTLEPG ADEAQLEALL VRELGRGANS PRALRKMHST
YTGLSLGDRG YVARVHPLEL WLVGYLRRHP GASLTEVLDA SVQERQDSYA WLFRTRHRSA
QDRRIRELVE GDAFAQIHRS WQRLGYPFAS LTPSYASAIG ASGDRPAALA ELMGILANDG
RRLPQPGVTA LHFARGTPYE TRLEQRGEAP QQVLAPEVAQ AARRALADVV RSGTARRLYG
AVIDADGRPI EITGKTGTGD RRFQVYGRGG RVIAERKVER TATFAFTLGD RYFGTLVAYA
REPYAARFRF TSALPVQLLK SLAPQLLPVL QQEGCSAPAG
//
