ID F3PFQ0_9BACE Unreviewed; 798 AA.
AC F3PFQ0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9445_00821 {ECO:0000313|EMBL:EGF54079.1};
OS Bacteroides clarus YIT 12056.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF54079.1, ECO:0000313|Proteomes:UP000010321};
RN [1] {ECO:0000313|EMBL:EGF54079.1, ECO:0000313|Proteomes:UP000010321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF54079.1,
RC ECO:0000313|Proteomes:UP000010321};
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., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-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=2.4.1.129;
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:EGF54079.1}.
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DR EMBL; AFBM01000007; EGF54079.1; -; Genomic_DNA.
DR AlphaFoldDB; F3PFQ0; -.
DR STRING; 762984.SAMN05444376_1717; -.
DR eggNOG; COG5009; Bacteria.
DR HOGENOM; CLU_006354_2_4_10; -.
DR Proteomes; UP000010321; 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 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 34..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 82..263
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 476..714
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 773..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 798 AA; 90921 MW; 458A702E120EBBFD CRC64;
MFGCIYIIFP YLCPIIIITE IVEPDMIKRV VKVLWIFIAL IALTCVIIFF SIAKGWIGYM
PPVEDLENPN YKFATEIFSE DGKVLGTYSY SKENRVFVGY NDLSPHIINA LIATEDVRFA
EHSGIDAIAL FRAVVKRGIL MQKNAGGGST ISQQLSKQLY SPSADNIMER LFQKPIEWVI
AVKLERYYTK EEILTMYLNK FDFLNNAVGI KTAAYTYFGC EPKELKIEEA ATLVGMCKNP
SLYNPVRYNE RSRGRRNVVL DQMRKAGYIT VEERDSLQAL PLKLSYHRVD HNEGLATYFR
EYLRGVLNAR KPDKSDYRGW QMQKYYEDSL DWETNPLYGW CEKNTKKDGS KYNLYTDGLK
IYTTIDSRMQ KYAEDAVTEH LKELQGYFFK EKKGAKKAPY TFRLTQEQVD EILGRAMRLS
DRYRIMKNAG ASEAEIKKAF DTPEQMSVFS WGGEKDTVMT PMDSIRYYKF FLRAGFMSMD
PRNGHVKAYV GGPNHHYFKY DMAMVGRRQI GSTMKPYVYS LAMENGFSPC DQARHVEYTL
IDENGKPWTP RNANKKRYGE MVTVKWGLAN SDNWITAYLM SKLNPYELKR LVHSFGVRNR
DIVPSVSLCL GPCEISVGEM VSAYTAFPNK GIRVAPLFVT RIEDNDGNVL ATFSPEMQEV
ISASSAYKML VMLRAVVNEG TGGRVRRLGV KADMGGKTGT TNFNADGWFM GFTPSLVSGC
WVGGEDRDIH FDTMLHGQGA SMALPIWAKY MVKVLGDKSL GYDENETFQL PEGFDPCKDS
DYEDAEPASE IGLDDLFN
//
