ID F4LNF7_TREBD Unreviewed; 776 AA.
AC F4LNF7;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 18-JUN-2025, entry version 73.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00044770};
DE EC=2.4.99.28 {ECO:0000256|ARBA:ARBA00044770};
GN OrderedLocusNames=Trebr_2509 {ECO:0000313|EMBL:AEE17915.1};
OS Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC Treponemataceae; Treponema.
OX NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE17915.1, ECO:0000313|Proteomes:UP000006546};
RN [1] {ECO:0000313|Proteomes:UP000006546}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC {ECO:0000313|Proteomes:UP000006546};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Treponema brennaborense DSM 12168.";
RL Submitted (APR-2011) 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=2.4.99.28;
CC Evidence={ECO:0000256|ARBA:ARBA00049902};
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; CP002696; AEE17915.1; -; Genomic_DNA.
DR RefSeq; WP_013759616.1; NC_015500.1.
DR AlphaFoldDB; F4LNF7; -.
DR STRING; 906968.Trebr_2509; -.
DR KEGG; tbe:Trebr_2509; -.
DR eggNOG; COG4953; Bacteria.
DR HOGENOM; CLU_006354_7_1_12; -.
DR Proteomes; UP000006546; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:TreeGrafter.
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:TreeGrafter.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:TreeGrafter.
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; IPR050396; Glycosyltr_51/Transpeptidase.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR009647; PBP_C.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
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 Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW ECO:0000313|EMBL:AEE17915.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006546};
KW Transferase {ECO:0000313|EMBL:AEE17915.1}.
FT DOMAIN 77..239
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 322..560
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 692..773
FT /note="Penicillin-binding C-terminal"
FT /evidence="ECO:0000259|Pfam:PF06832"
SQ SEQUENCE 776 AA; 83216 MW; 5B4482F52C5D5DF0 CRC64;
MSLRKNNGAG NSQAAKFAGR RRRIAAAVVA VIALWGGVRL TLRFAPFAAL DAFIVRPCST
RVYDRNGVLL QVLPLENGLR REWYDLDALP PAILRVFIAA EDENFYRHGG VDVIALVRAF
VQNAKSGRPV SGASTVTMQL ARLVVPRDPG KPVSVGVKLA EAFTAVRIES KLPKKRILEL
YLNSLPFGLQ AEGVGSAART YFGTTPDRLS EAQIHALAVI PRRPVKYNPL EDPGASFEAA
AEIGKRTGFS VTKTEWIDAV SVGERYEYPL GMPHFVLYVR NSAGGRLPPE LHTSVDAALS
DKVANDISTQ IALHADARLS HGAALVIDNV TGEILCWAGS GDFFSENEGQ IDGVLVRNQS
GSTMKPFIYA LALERGFTPS SVLADVPMDF GSEQVYVPLN FNNQYNGPVL LRNALASSLN
IPAVYLLYRL GVDNYLKTLG ALGFDSLAGE RNRQGLSLAL GSGEVTLFEL VRAFSVFARG
GTIPSVTYLK AGAVSAEAGT EPAGLADFSA SAAVYEPDTA ALICDILSDR RARALGFGFA
EVFSTPYPAI FKTGTSNQFQ NIIALGSTAR YTAGVWMGNF TGETVVRETG SSVPAAVVRG
VLDVLSERNP ETAAAFAAPR NYRKLPVCAV SGMAPGPDCP AVTDEYVALA AAANRPVCSW
HYRQNGRVHV RYPQEYQRWL SGRNTAGALA DTGEGRILYP ADGAVFVFDP SIPSAAQKIK
VDCTGAGARA ELFVNGVSAG TSERPFSWYV PLLPGEMRLT VRFADGRNAA IRISVK
//
