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Database: UniProt
Entry: D3IAN6_9BACT
LinkDB: D3IAN6_9BACT
Original site: D3IAN6_9BACT 
ID   D3IAN6_9BACT            Unreviewed;       836 AA.
AC   D3IAN6;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, 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=HMPREF0669_00490 {ECO:0000313|EMBL:EFC71818.1};
OS   Prevotella sp. oral taxon 299 str. F0039.
OG   Plasmid unnamed {ECO:0000313|EMBL:EFC71818.1}.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575614 {ECO:0000313|EMBL:EFC71818.1, ECO:0000313|Proteomes:UP000015929};
RN   [1] {ECO:0000313|EMBL:EFC71818.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC71818.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=unnamed {ECO:0000313|EMBL:EFC71818.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA   Yandava C., Izard J., Baranova O.V., Blanton J.M., Tanner A.C.,
RA   Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EFC71818.1, ECO:0000313|Proteomes:UP000015929}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0039 {ECO:0000313|EMBL:EFC71818.1,
RC   ECO:0000313|Proteomes:UP000015929};
RC   PLASMID=Plasmid {ECO:0000313|Proteomes:UP000015929};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA   Blanton J.M., Tanner A.C., Dewhirst F.E., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. Oral Taxon 299 strain F0039.";
RL   Submitted (JUN-2012) 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}.
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DR   EMBL; CP003667; EFC71818.1; -; Genomic_DNA.
DR   RefSeq; WP_009227666.1; NC_022111.1.
DR   AlphaFoldDB; D3IAN6; -.
DR   KEGG; pro:HMPREF0669_00490; -.
DR   HOGENOM; CLU_006354_2_4_10; -.
DR   OrthoDB; 9766909at2; -.
DR   Proteomes; UP000015929; Plasmid.
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   Plasmid {ECO:0000313|EMBL:EFC71818.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015929};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        32..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          89..274
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          448..684
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          792..836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        792..828
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   836 AA;  95188 MW;  D0F166C57C9318D1 CRC64;
     MIDKIKKIFS ILLQKIKDFF NWYKKLFVGR AWYIKALSGI ASFFVFIAIY LIAVDVNFLW
     LFGKSPGFSE IKKPSTSEAS EIYSADGVLI GKYFNENRTP VKYSDVNPIF WKTLIDTEDE
     RFYHHFGIDI PGLFAAAKDA IFRHDARGAS TITQQLAKNM FRVRTNYSTG LLGSIPGIRM
     LIMKSKEWII ATKLEMVYDK EDILTMYANT VDFGANSYGI KTASKTYFNT SPKDLTIEQS
     AVLVGMLKAT TSYNPITNPE NSLKRRNTVL WRMHQHNDIT KAEYDSLTQI PIKLDVKVEK
     NYDGQAQYFR EAVADHLKDW CDENGIDLYS SGLKIYTTID SRMQKYAEDA ARKQMRQVQR
     NFNNHWGDND PWIDENGNKI PNFIENIAQK QPYYKYLLAK FPNNPDSISY YLNKPHVVKL
     FDYDKGIIEK EISTMDSIRY MVHFMHCAFV AMEPQTGEVK AWVGDIDFNS WKYDKVTAMR
     QPGSTFKLFV YTEAMNQGLT PCDKRRDEFI SMKVFDKKKG EEVTWTPSNA NGRFSGDSIP
     LKGAFARSIN SVAVRLGQEM GIQRVIETAQ KMGIKSPLDP TPSLALGSSD INLLELTNAY
     SVIADDGKHH DPILVTRILD KEGHEVYVAP TSETQVISYK SAFFMQQLLM GGMREPGGTS
     QSLWAYVGDY RDTDFGGKTG TSNNHSDAWF MCVSPKLVCG AWVGGEYRSI HFRTGALGQG
     SRTALPICGY FLQSVFGDSA FKKYHGQFGK PKDDDITSSM YNCQSYYSSS RRDTTVTDST
     NISHEEIILD EDGNIRITPN EGTKHESRPT NEKEQNPRSD KQNKKNKEQV VNFEQL
//
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