ID A0RBR2_BACAH Unreviewed; 680 AA.
AC A0RBR2;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbp2A {ECO:0000313|EMBL:ABK84655.1};
GN OrderedLocusNames=BALH_1310 {ECO:0000313|EMBL:ABK84655.1};
OS Bacillus thuringiensis (strain Al Hakam).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=412694 {ECO:0000313|EMBL:ABK84655.1, ECO:0000313|Proteomes:UP000000761};
RN [1] {ECO:0000313|EMBL:ABK84655.1, ECO:0000313|Proteomes:UP000000761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Al Hakam {ECO:0000313|EMBL:ABK84655.1,
RC ECO:0000313|Proteomes:UP000000761};
RX PubMed=17337577; DOI=10.1128/JB.00241-07;
RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D.,
RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C.,
RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A.,
RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D.,
RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.;
RT "The complete genome sequence of Bacillus thuringiensis Al Hakam.";
RL J. Bacteriol. 189:3680-3681(2007).
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; CP000485; ABK84655.1; -; Genomic_DNA.
DR RefSeq; WP_000769278.1; NC_008600.1.
DR AlphaFoldDB; A0RBR2; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; btl:BALH_1310; -.
DR HOGENOM; CLU_006354_2_2_9; -.
DR Proteomes; UP000000761; 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 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 Glycosyltransferase {ECO:0000313|EMBL:ABK84655.1};
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 Transferase {ECO:0000313|EMBL:ABK84655.1};
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 641..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 680 AA; 77033 MW; CA67465CBD4F2987 CRC64;
MKLKNTHLKK MQEWFNKRKK LRNSLIILGS LLATLFIAIN IIISIQDISE LKQAVPQPTL
IYDANNEVAT KLASSKTEGV KKKDIPDIMV QAIVAVEDKE FFNHHGIYYS GIISAVFKNI
TAGEVVAGGS TITQQLAKNV FLTQDRTYSR KIKEYFLTKK IERTYTKDEI IEMYMNQIYF
GEGAWGIKRA AKSYFDKDVK DLTISEAATI AGLIKAPSAY SPYKNFNKSI ERRNVVLSLM
KEQGYISDEQ YNKEKESGLV LKRGVDDKYK GKYSQYVDYI VREAMDKYEL TQNEILAGGY
RIYTELDPKK QQAVEDVVNN NSYFKDSGSD QLMQTGVVLM NPKTGGVPAL VGGRGPYQFL
QFNHATQLKR QPGSTLKPLA VYVPALEQGY EVYDILKDEP FNIKEYKPQN SDHTFHGDVT
MYEAVAKSYN VSAVWLLEQI GLDKGLKSLE RFGIPLVPED RTYPIALGGM HVGTSPFVMA
QAYSTFANDG VQVEAHAIRE IQNAEGETIG KWYKKETRVT SEKTSQKMTY LLKGVVEKGT
GEKAKVTNVD TAGKTGTTQI VNGPSTGAKD SWFVGYTPDL VGAIWVGYDK TDSDHYVPGG
SQITTTMFRD IMKKANANPA QKAFQLSLIS EADYKKQLTT IEEEKRRKEE EKRRKEEEQQ
RKQEQQEWLD KVKEWIPSFW
//
