ID A0A1I1L1I7_9BURK Unreviewed; 736 AA.
AC A0A1I1L1I7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=SAMN05216321_10612 {ECO:0000313|EMBL:SFC66904.1};
OS Cupriavidus sp. OV038.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1855313 {ECO:0000313|EMBL:SFC66904.1, ECO:0000313|Proteomes:UP000199583};
RN [1] {ECO:0000313|EMBL:SFC66904.1, ECO:0000313|Proteomes:UP000199583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV038 {ECO:0000313|EMBL:SFC66904.1,
RC ECO:0000313|Proteomes:UP000199583};
RA de Groot N.N.;
RL Submitted (OCT-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; FOKX01000006; SFC66904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1L1I7; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000199583; 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..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..736
FT /note="peptidoglycan glycosyltransferase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011475344"
FT DOMAIN 50..224
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 313..558
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 633..715
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 736 AA; 78629 MW; D596A6A8772698F0 CRC64;
MTMPRRLFAP LVLLALAAAT SSAAAVPAFR DVRDNWRSAD IVVMDRHGEP VARVRDDFRA
RRGDWVTLAD TSPALRTAIV LSEDRRFYAH SGVDWQGVAA AAWANMWNTR TRGASTLTMQ
LAGLLDEDLR AARGRSFGQK VGQAVSAASL EHGWSKDQIL EAYLNLVPFR GELVGLSAMS
QTLFGKVPSG LNAREAALAV ALVRGPNAAP GQVSVRACRI LREMKQPREC DGLDGFTALA
LAKSASVPDA SFRTNLAPHL ARAVIAHTRE TLPAGRPVPA RIASTVDAEV QRVAVDSLSR
HLRELAGRNA EDGAVVVIDN ASGDVLAYVG SSGALSSAAQ VDHAAAPRQA GSTLKPFLYA
QAIEERRLTA ASLLDDRPVN LPTGGGLYIP QNYDHRYAGW VSLRAALGSS LNVPAVRTLV
MVTPHRFHRR LVALGLPLTE SGDYYGYSLA LGSADVSLLS LTNAYRSFAN QGAYGPVRMT
VDGATVPRQP VMSPAASYVI GDVLADRHAR ARTFGLDSPL TTRFWTAVKT GTSKDMRDNW
CIGWSQRYTV GVWIGNASGA SMHDVSGVSG AAPVWHDVMA ALHRQSSSRA PAMPAGVERV
PLTFADNLEP AREEVFLAGT AVTRINVGAA PPSSGTPAIA SPRDGTIFAL DPDIPPDAQR
VWFHADGLTG QTARAVSWRI DGKPLGKGGQ LAWLPWPGRH RVELVDAAGK VVDDIGIEVR
GASVREAGPQ RTSMRR
//