ID G6AGK6_9BACT Unreviewed; 784 AA.
AC G6AGK6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=HMPREF9138_01202 {ECO:0000313|EMBL:EHG16040.1};
OS Prevotella histicola F0411.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=857291 {ECO:0000313|EMBL:EHG16040.1, ECO:0000313|Proteomes:UP000004597};
RN [1] {ECO:0000313|EMBL:EHG16040.1, ECO:0000313|Proteomes:UP000004597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0411 {ECO:0000313|EMBL:EHG16040.1,
RC ECO:0000313|Proteomes:UP000004597};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Ganesan A.,
RA Blanton J.M., Baranova O.V., Tanner A.C., Mathney J.M.J., Dewhirst F.E.,
RA Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A.,
RA Alvarado L., Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z.,
RA Dunbar C., Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella histicola F0411.";
RL Submitted (OCT-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:EHG16040.1}.
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DR EMBL; AFXP01000010; EHG16040.1; -; Genomic_DNA.
DR AlphaFoldDB; G6AGK6; -.
DR STRING; 857291.HMPREF9138_01202; -.
DR PATRIC; fig|857291.3.peg.1201; -.
DR HOGENOM; CLU_006354_2_4_10; -.
DR Proteomes; UP000004597; 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 Reference proteome {ECO:0000313|Proteomes:UP000004597};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..255
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 468..705
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
SQ SEQUENCE 784 AA; 89480 MW; 2985CEAD1B25FFB0 CRC64;
MLIHSFTLSL HNIFHKFMRR HFVHFLWGSL IAVLGFIFVF FISVWNGWVG YMPDMDELSN
PIDKFASQVY SSDQQLIGTW NQDNNNRVAI DYNGLSPHLV HALVATEDER FYEHSGIDFI
ALGRAIIKRG VMRQASAGGG STITQQLAKQ LFSEKAHSTL ERLLQKPIEW IIAVKLERHF
TKEEILAMYF NYFDFLHNAV GIKRAANVYF NKEPRNLTVT EAALLVGLCK NPSMFNPLRH
PERCLQRRNV VLMQMVKSGY VTKAEYAELS QRPLGVHFTK AKPINGSADY FQAFLRQYMM
EKKPERDNYQ AWQARQFVLD SIAWEQDPLY GWCNKNMKRN GEPYNVNTDG LRIYTTIDTR
MQQYAEEAVR KHVGGYLQAQ FNQAMRYKKD APFSSNISHR TIKQILNRAC RQSLRYRRMK
EQGATPEEIK RSFRTPHEMT IFTYHGDIDT VMTPIDSIRY YKSFLRAAFM SMDPHTGAVK
AYVGDIDYQH FKYDVVMGGR RQVGSTIKPF LYALAMQNGM TPCTLAPNVQ RTYGGWTPRN
GSHARYGQEV PLRWGLQQSN NWISAYLINL LGPTQFVNIL HDFGLNNPDI DKNTSPVLSL
GPCEVSVGEM TSAYTTFANG GIRCSPLFVT KIEDSHGNVI AKFQPLMTEV ISEISSYQMI
DMLRAVIEGG TASRLRYAYH LTGDIGGKTG TTNNNSDGWF LGITPELVSG CWVGGEDRDI
HFDNTSMGQG ATTALPVWAY YMQKVFADHR LGYNPNKKFA IPAKFNPCQT ADTINVNGIQ
EEYF
//
