ID C9LE04_9BACT Unreviewed; 800 AA.
AC C9LE04;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=GCWU000325_00427 {ECO:0000313|EMBL:EEX72659.1};
OS Alloprevotella tannerae ATCC 51259.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=626522 {ECO:0000313|EMBL:EEX72659.1, ECO:0000313|Proteomes:UP000003460};
RN [1] {ECO:0000313|EMBL:EEX72659.1, ECO:0000313|Proteomes:UP000003460}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51259 {ECO:0000313|EMBL:EEX72659.1,
RC ECO:0000313|Proteomes:UP000003460};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX72659.1}.
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DR EMBL; ACIJ02000009; EEX72659.1; -; Genomic_DNA.
DR RefSeq; WP_006254201.1; NZ_GG700642.1.
DR AlphaFoldDB; C9LE04; -.
DR STRING; 626522.GCWU000325_00427; -.
DR GeneID; 84575691; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_10; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000003460; 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; 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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000003460};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..237
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 451..691
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 743..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 800 AA; 90231 MW; A94AC7BD81B87C83 CRC64;
MQKKVLGILW TIYGCIVLLI IGATFSIERG WIGYMPPLDE LQNPIDKYAS QVFSADGKVL
GTWSQNENRI FTDYDSISSH MFDALIATED VRFYQHSGID AKAFGRAVVK RGFLGQRAAG
GGSTITQQLA KQLYSKRAHS TLGRLFQKPI EWVIAVELER HFTKKEILTL YLNYFDFLHN
AVGIKTAAKV YFQKTPQQLT ITEAAMLVGM CKNPSYYNPI TAPDRCKQRR NVVLDQMVKG
GYLNASEAVT LKEEPLGLHF KRIDHKNGPA TYLREYLRRI LMADKPKKEN YADWQQVQYF
GDSLSWANDP LYGWCKKNVK RDGTNYDIYT DGLKIYTTID SRMQRYAEEA AYSHVAKYLQ
PLFYREKKGS SSFPFSSKLT RKQIMSILAR SELQSERYRM LKDAGASEEE IRKSFHTKIR
MSIFSYRGTI DTMMTPLDSI RYYKSFLRTG LVSIDPSSGQ VKAYVGGLNY NYFQYDMAFV
GRRQIGSTMK PFVYSLAMED GLTPSYTIPN VMRTYMVAGR AWTPRNGSKA RYGSSVPLSW
GLAQSNNWVT AGLMSQIDPT GHRLAKIMKD YGVKNPNIYP SIALCLGPCD VTVGELASAY
TAFANGGIRV APLLVTKIED AQGNVIAEFS PRVNEVISEE SADEMITMLR GVVQSGTAGR
LRYKYNLNGP IAGKTGTTNN NSDGWFVGLV PRLVTACWVG GEDRDIHFDR TNSGQGATVA
LPIWAYYMKK VYRDHSLGYK ENEEFKKSVR PKTSPTPSVQ GNNMTDDEET PDPEPQPQRN
TEAPPPKRTA NQPRGESLFE
//
