ID M6UF82_9LEPT Unreviewed; 805 AA.
AC M6UF82;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=LEP1GSC187_2494 {ECO:0000313|EMBL:EMO43752.1};
OS Leptospira santarosai str. ZUN179.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=1049985 {ECO:0000313|EMBL:EMO43752.1, ECO:0000313|Proteomes:UP000012160};
RN [1] {ECO:0000313|EMBL:EMO43752.1, ECO:0000313|Proteomes:UP000012160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZUN179 {ECO:0000313|EMBL:EMO43752.1,
RC ECO:0000313|Proteomes:UP000012160};
RA Harkins D.M., Durkin A.S., Brinkac L.M., Haft D.H., Selengut J.D.,
RA Sanka R., DePew J., Purushe J., Matthias M.A., Vinetz J.M., Sutton G.G.,
RA Nierman W.C., Fouts D.E.;
RL Submitted (JAN-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 -!- 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:EMO43752.1}.
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DR EMBL; AHOQ02000049; EMO43752.1; -; Genomic_DNA.
DR RefSeq; WP_004484107.1; NZ_AHOQ02000049.1.
DR AlphaFoldDB; M6UF82; -.
DR Proteomes; UP000012160; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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: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; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF11; PENICILLIN-BINDING PROTEIN 1B; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 93..268
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 415..673
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 763..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 90171 MW; 8BD7C16FD5153CC0 CRC64;
MTSGNEKISS VFNSLRGGFV SLFLFIKSYW RFVFRYAVIA AVVTVSFLIG GSYVVWLTKK
DEIVSNLDKF KNEVTNYYEI SQIRPIRILD RNGKLIGEFS RRKFKPIRTD NLAEHGNVVW
ALLSSEDREF YNHHGVNYAA LLRAIIINLT TFQKQGGSTI TQQLAKLTLD LGARNIFNKI
TEFYCTFYLE SQFDKNTILS MYLNRIFLGE GNTGVEEASR YYFNKAASEL TPEEAAMLVG
IIPAPSNYNP VRSLKIALKR QKLVLTPMSE NQHLHPDPSS IEKNFSRKID TNLKKFKTFY
NVELTKDGEK EFYSSDIARY GFDKDFTINL APDFNYGIRQ NILDTFSEID IETRGMNVYT
TLDYAKQDVA EKSLREGIES VRKKLNDVKA VYAKKGNSEE ARVQQSIIDN MNGSLISINP
GNGHIEAMVG SYKISNIFRL NRAVSALRQP GSTIKALIYA IAFENRIITP SSNVVDEEIN
IRGYSPKNWY KGYKGEITAR IAFAQSVNTI AVKLLNEFGV SVFLEKISMI LDVDKTTLEK
RFQPNLSLAL GSGELSPMEL ALIYATIANG GKKITPVQIL RITDFEGSEM FSAPLKDPNE
TIQILDPVAC AETINLLEAV LSEQGTMKLK LKDEDFFPMG GKTGTVQSPK EARKKWGSRK
GVRDAWFAGV NPDLVTTVWI GNDVGAPFEG SGSGISGNIW FRYVNYIAKN IGFSETLVKP
FNGDFVRVDV CGETGLLLHS SVPCLYPLYG QYYYIGEQPS APAAATSENS AQETTTEKAI
LPQEEENDSD SVELELPEIT DNPPN
//
