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
//