ID E5V9H6_9BACE Unreviewed; 776 AA.
AC E5V9H6;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=DXB40_12520 {ECO:0000313|EMBL:RGN82628.1}, HMPREF1007_01409
GN {ECO:0000313|EMBL:EFV26499.1};
OS Bacteroides sp. 4_1_36.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=457393 {ECO:0000313|EMBL:EFV26499.1, ECO:0000313|Proteomes:UP000004735};
RN [1] {ECO:0000313|EMBL:EFV26499.1, ECO:0000313|Proteomes:UP000004735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4_1_36 {ECO:0000313|EMBL:EFV26499.1,
RC ECO:0000313|Proteomes:UP000004735};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Young S.K., Gargeya S., Zeng Q.,
RA Alvarado L., Berlin A., Bochicchio J., Chapman S.B., Chen Z., Freedman E.,
RA Gellesch M., Goldberg J., Griggs A., Gujja S., Heilman E., Heiman D.,
RA Howarth C., Mehta T., Neiman D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., White J., Yandava C.,
RA Allen-Vercoe E., Sibley C., Strauss J., Daigneault M., Haas B., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 4_1_36.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RGN82628.1, ECO:0000313|Proteomes:UP000261007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OM03-9 {ECO:0000313|EMBL:RGN82628.1,
RC ECO:0000313|Proteomes:UP000261007};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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:EFV26499.1}.
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DR EMBL; ACTC01000057; EFV26499.1; -; Genomic_DNA.
DR EMBL; QSUY01000026; RGN82628.1; -; Genomic_DNA.
DR RefSeq; WP_005829073.1; NZ_GL622501.1.
DR AlphaFoldDB; E5V9H6; -.
DR HOGENOM; CLU_006354_2_4_10; -.
DR Proteomes; UP000004735; Unassembled WGS sequence.
DR Proteomes; UP000261007; 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.
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 9..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 57..238
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 451..690
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 776 AA; 88480 MW; 3EA168AB5E93D025 CRC64;
MIRKVVKILW IFIALISLVC VFIFFSIAKG WIGYMPPVED LENPNYKFAT EVFSEDGKVL
GTYSYSKENR VFVGYNDLSP NIINALIATE DVRFAEHSGI DAYALTRAVV KRGILMQKNA
GGGSTITQQL SKQLYSPSAD NVMERLFQKP IEWVIAVKLE RYYTKEEILT MYLNKFDFLN
NAVGIKTAAF TYFGCEPKDL KIEEAATLVG MCKNPSLYNP VRYNERSRGR RNVVLDQMRK
AGYITEAERD SLQALPLKLK YNRVDHKEGL ATYFREYLRG VLTAKKPDKA NYRGWQMQKY
YEDSLDWENN PLFGWCEKNT KKDGTKYNLY TDGLKIYTTL DSRMQQYAED AVTEHLKELQ
GYFFKEKKGA KKAPYTFRLT QEQVDEILGR AMRLSDRYRI MKKAGATEAE IKKAFDTPEE
MSVFSWEGEK DTIMTPMDSI RYYKFFLRAG FMSMDPRSGH VKAYVGGPNY HYFQYDMAMV
GRRQVGSTIK PFLYTLAMEN GFSPCDEVRH VEYTLIDENG KPWTPRNANK KLIGDMVTVK
WGLANSDNWI TAYLMSKLNP YNLKRLIHTF GVRNRDIVPS VSLCLGPCEI SVGEMVSAYT
AFPNKGIRVA PLFVTRIEDN DGNVLATFAP EMQEVISVSS AYKMLVMLRA VVNEGTGGRV
RRLGVKADMG GKTGTTNYNA DGWFMGFTPS LVSGCWVGGE DRDIHFDTML HGQGASMALP
IWTKYMVKVL GDKSLGYDEN ETFQLPEGYD PCKDDVNLEG DTHIEEPIEG LDELFN
//
