ID Q6HJ27_BACHK Unreviewed; 834 AA.
AC Q6HJ27;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 107.
DE RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN Name=pbp1A {ECO:0000313|EMBL:AAT59830.1};
GN OrderedLocusNames=BT9727_2122 {ECO:0000313|EMBL:AAT59830.1};
OS Bacillus thuringiensis subsp. konkukian (strain 97-27).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=281309 {ECO:0000313|EMBL:AAT59830.1, ECO:0000313|Proteomes:UP000001301};
RN [1] {ECO:0000313|EMBL:AAT59830.1, ECO:0000313|Proteomes:UP000001301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=97-27 {ECO:0000313|EMBL:AAT59830.1,
RC ECO:0000313|Proteomes:UP000001301};
RX PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S., Brown N.,
RA Bruce D., 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., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., Okinaka R.T.,
RA Parson-Quintana B., Reilly L.P., Richardson P., Robinson D.L., Rubin E.,
RA Saunders E., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Ticknor L.O., Wills P.L., Brettin T.S., Gilna P.;
RT "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT thuringiensis isolates closely related to Bacillus anthracis.";
RL J. Bacteriol. 188:3382-3390(2006).
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; AE017355; AAT59830.1; -; Genomic_DNA.
DR RefSeq; WP_001293985.1; NC_005957.1.
DR RefSeq; YP_036449.1; NC_005957.1.
DR AlphaFoldDB; Q6HJ27; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; btk:BT9727_2122; -.
DR PATRIC; fig|281309.8.peg.2232; -.
DR HOGENOM; CLU_006354_3_0_9; -.
DR OMA; LAQMAMI; -.
DR Proteomes; UP000001301; 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:SF29; PENICILLIN-BINDING PROTEIN 1A/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 Glycosyltransferase {ECO:0000313|EMBL:AAT59830.1};
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:AAT59830.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 37..60
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..260
FT /note="Glycosyl transferase family 51"
FT /evidence="ECO:0000259|Pfam:PF00912"
FT DOMAIN 351..634
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 640..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 738..834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 91748 MW; 9D014AEA26D02A4A CRC64;
MSENYRSREE RRQVKKKKQP ASKTQKPKGK TSFFRKFLIT CLLLGIVGLV GGVATFFVMI
KDAPKLEKAK LVNPLSSKIY DKNGDLVYEY GKEKRTNVTY DQIPKLVENA FLATEDARFY
EHSGVDFKGT ARAVLVSLKG DYGSQGGSTI TQQVIKNYFL SMEKTSKRKI QEIYLAYKLE
QQYSKHEILE MYLNKINLGN RSYGIATAAQ NYYGKELKEL TLPEVAMLAG LPKAPNNYDP
TKTENVQRAT ERRNVVLKLM NRHGYITKAE MEEASKVEVT DGLKTATVQA MPYPAFMDAV
VKEVEKELPD ANIGSDGLEI YTTLDIDAQK AADRILDANI INYPNDKFQS AFTFMDTKTG
EVRAIGSGRG ENKAVFKGHN MAIELDRAAG STMKPIFDYG PAIEYLKWAT YHQIDDSPFK
YSTGQEVRNA DRSHLGSITM REALKMSRNV PAVKTAKEVG LNKAKEFSEK LGITLKSVPE
STAIGTNEVS PTEIAGAYAT FGNGGKYAKP HFVKKVVYPD GKSQSFGQKP KQVIADSTAY
MITDMLRSVV TSGTGTAANI SSLDVAGKTG TTNYDSKQLA KFNIPESATR DSWFAGYTPQ
YTMAVWTGYM KDGKDEYISS KNTKIAQLIF KEMMSEMATD KSRFKMPSSV IQEGSELRIK
GEKRDSSPNT SVPDTTEKPK QDQQQKTEEE KKQEELKKQE ELKKQEEEKK QEELKKQEEQ
KKLEEQKKQE EEKKQNEQNN GNGQGTTPPA NNGGGQGNTT PPANNGGGQG NTTPPANNGG
GQGNTTPPAN NGGGQGNTTP PANNGGGQGN TTPPATTQPE TGGNAGEAPA NNGQ
//