ID J8DKM4_BACCE Unreviewed; 680 AA.
AC J8DKM4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN ORFNames=IGC_04027 {ECO:0000313|EMBL:EJQ76799.1};
OS Bacillus cereus HuA4-10.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1053206 {ECO:0000313|EMBL:EJQ76799.1, ECO:0000313|Proteomes:UP000006977};
RN [1] {ECO:0000313|EMBL:EJQ76799.1, ECO:0000313|Proteomes:UP000006977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HuA4-10 {ECO:0000313|EMBL:EJQ76799.1,
RC ECO:0000313|Proteomes:UP000006977};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Feldgarden M., Van der Auwera G.A., Mahillon J., Duprez V., Timmery S.,
RA Mattelet C., Dierick K., Sun M., Yu Z., Zhu L., Hu X., Shank E.B.,
RA Swiecicka I., Hansen B.M., Andrup L., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus cereus HuA4-10.";
RL Submitted (APR-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 -!- 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:EJQ76799.1}.
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DR EMBL; AHEA01000027; EJQ76799.1; -; Genomic_DNA.
DR RefSeq; WP_002149441.1; NZ_JH792148.1.
DR AlphaFoldDB; J8DKM4; -.
DR PATRIC; fig|1053206.3.peg.4107; -.
DR HOGENOM; CLU_006354_2_2_9; -.
DR Proteomes; UP000006977; Unassembled WGS sequence.
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 2A; 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 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 69..240
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 336..613
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 643..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 77194 MW; E83B93675EE08E2A CRC64;
MKLKNTHLKK TLEWFNKRKK LRNSLIVLGS LLATLFIVVN IIISIQDISE LKQAVPQPTL
IYDANNEVAT KLASSKTEGV KRKDIPDIMV QAIVAVEDKE FFSHHGIYYS GIISAVFKNI
TAGEVVAGGS TITQQLAKNV FLTQDRTYSR KIKEYFLTKK IERTYSKDEI IEMYMNQIYF
GEGAWGIKRA AKSYFDKEVK DLTISEAATI AGLIKAPSAY SPYKNFNKSI ERRNVVLSLM
KEQGYISEEQ YNQEKESGLV LRRGVDDKYK GKYSQYVDYI VREAMDKYEL TQNEILAGGY
RIYTELDPKK QQAVEDVVNN DSYFKDSGSD QLMQTGVVLM NPKTGGVPAL VGGRGPYQFL
QFNHATQLKR QPGSTLKPLA VYVPALEQGY EVYDVLKDEP FNIKEYAPQN SDHTFHGNVT
MYEAVAKSYN VSAVWLLEQI GLDKGLKSLE RFGIPLEPED RTYPIALGGM HVGTSPFVMA
QAYSTFANDG VQVEAHAIRE IQNAEGETIG KWYKKETRVT SEKIAQKMTY LLKGVVEKGT
GEKAKVNNVD TAGKTGTTQI VNGPRNGAKD SWFVGYTPDL VGAIWVGYDK TDSEHYVPGG
SQITTTMFRD IMKKANVNPA QKAFQLSLIP EADYKKQLQT IEEEKRRKEE EKRRKEEEQQ
RKQEQQEWFD KVKEWIPSFW
//
