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Database: UniProt
Entry: B7HGF8_BACC4
LinkDB: B7HGF8_BACC4
Original site: B7HGF8_BACC4 
ID   B7HGF8_BACC4            Unreviewed;       705 AA.
AC   B7HGF8;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   Name=pbpF {ECO:0000313|EMBL:ACK60339.1};
GN   OrderedLocusNames=BCB4264_A1102 {ECO:0000313|EMBL:ACK60339.1};
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532 {ECO:0000313|EMBL:ACK60339.1, ECO:0000313|Proteomes:UP000007096};
RN   [1] {ECO:0000313|EMBL:ACK60339.1, ECO:0000313|Proteomes:UP000007096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264 {ECO:0000313|EMBL:ACK60339.1,
RC   ECO:0000313|Proteomes:UP000007096};
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) 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};
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DR   EMBL; CP001176; ACK60339.1; -; Genomic_DNA.
DR   RefSeq; WP_000756292.1; NC_011725.1.
DR   AlphaFoldDB; B7HGF8; -.
DR   CAZy; GT51; Glycosyltransferase Family 51.
DR   KEGG; bcb:BCB4264_A1102; -.
DR   HOGENOM; CLU_006354_2_2_9; -.
DR   OMA; YVKNAML; -.
DR   Proteomes; UP000007096; Chromosome.
DR   GO; GO:0016020; C:membrane; 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:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase 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; 1.
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   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF32; PENICILLIN-BINDING PROTEIN 1F; 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        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          51..225
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          317..589
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   705 AA;  79690 MW;  9C4A3F9BB1D2E1ED CRC64;
     MKKVKWTLLG GVATFVVAIV IYKLIVLAGG YMMDEKQLVF HSSSRIVDQK GKEITKLYVE
     NRELVPIEQI PKYVQQAFVA VEDSRFYEHQ GIDYPSIFRA LYKDTLAREK VEGGSTITQQ
     LAKNVFLTRE KTFTRKLKEV AISLQLEQKY TKQQILEMYM NHIYFGHGAY GIQAAAKLYF
     NKNVEDLTVE EGAMLAGLPK SPNGYSPYYS AEKSKERRDL VLSLMHKQGY LTAEESVRYQ
     GKTIALYKNL DENELAYMPY IDMVIDEAAR LYGLSHQEVL RGGYTFVVPM DEKIQKVAYN
     QFQDARNFPG KEEGAQGAFL LMDNRTGGIK AAIGGRKYVP RGFNRVFAKR QPGSVLKPLI
     VYAPALETKK YNPYSLLTNE RNSFEGYEPR NYNHEYSKEM TMYDAILESA NVPAVSLLNE
     LGVEEGKQYL EKGNVHIADA GLSTALGGLK NGVSTFDLVK MYRSFLANGN IIEPHVIDKV
     LNRHGAVIGE SPKVETKIFS KQTAWYMTKM LEGVVKEGTA RVGVYNGALA GKTGTTSLPN
     DDKGARDMWF VGYTPNLVGA VWIGYDRTDK EHQLQGESAS ATKLFKKILT KSNVEHKEKF
     MKPEGVETIS APIRLRKIED VKMKLSFSPF GLFKAKLSWT PLPDNRIMYR IYRVENGIHT
     HVSTVNGAGE YEEKFVNIFS KPSFYVVPYN TQTNREGEKS KVAKP
//
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