ID B0NP86_BACSE Unreviewed; 775 AA.
AC B0NP86;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=BACSTE_01332 {ECO:0000313|EMBL:EDS15887.1};
OS Bacteroides stercoris ATCC 43183.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=449673 {ECO:0000313|EMBL:EDS15887.1, ECO:0000313|Proteomes:UP000004713};
RN [1] {ECO:0000313|EMBL:EDS15887.1, ECO:0000313|Proteomes:UP000004713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43183 {ECO:0000313|EMBL:EDS15887.1,
RC ECO:0000313|Proteomes:UP000004713};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Bacteroides stercoris(ATCC 43183).";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDS15887.1, ECO:0000313|Proteomes:UP000004713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43183 {ECO:0000313|EMBL:EDS15887.1,
RC ECO:0000313|Proteomes:UP000004713};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (NOV-2007) 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:EDS15887.1}.
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DR EMBL; ABFZ02000018; EDS15887.1; -; Genomic_DNA.
DR RefSeq; WP_005654014.1; NZ_DS499672.1.
DR AlphaFoldDB; B0NP86; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR GeneID; 31796760; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_10; -.
DR Proteomes; UP000004713; 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"
FT REGION 746..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 775 AA; 88310 MW; 43E9C33A906189BC CRC64;
MIKKVVKVLW IFIALITLTC VVIFFSIAKG WIGYMPPVED LENPNYKFAT EIFSEDGKVL
GTYSYSKENR VFVGYNDLSP HIINALIATE DVRFAEHSGI DAIALFRAVV KRGILMQKNA
GGGSTISQQL SKQLYSPSAD NIVERLFQKP IEWVIAVKLE RYYTKEEILT MYLNKFDFLN
NAVGIKTAAY TYFGCEPKDL KIEEAATLVG MCKNPSLYNP VRYNERSRGR RNVVLDQMRK
AGYITVEERD SLQALPLKLS YHRVDHNEGL ATYFREYLRG VLNAKKPDKS DYRGWQMQKY
YEDSLDWETN PLFGWREKNT KKDGSKYNLY TDGLKIYTTI DSRMQKYAED AVTEHLKELQ
GYFFKEKKGA KKAPYTFRLT QEQVDEILDR AMRLSDRYRI MKRTGASEAE IRKAFDTPEQ
MSVFSWSGEK DTVMTPMDSI RYYKFFLRAG FMSMDPRNGH VKAYVGGPNH HYFKYDMAMV
GRRQIGSTMK PYVYSLAMEN GFSPCDQARH VEYTLIDENG KPWTPRNANK KRYGDMVTVK
WGLANSDNWI TAYLMSKLNP YELKRLVHSF GVRNREIVPS VSLCLGPCEV SVGEMVSAYT
AFPNKGIRVA PLFVTRIEDN DGNVLATFSP EMQEVISASS AYKMLVMLRA VVNEGTGGRV
RRLGVKADMG GKTGTTNYNA DGWFMGFTPS LVSGCWVGGE DRDIHFDTML HGQGASMALP
IWAKYMVKVL GDKSLGYDEN ETFQLPEGFD PCKDSGYEDA DAEPASEMGL DDLFN
//
