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Database: UniProt
Entry: Q6HJ27_BACHK
LinkDB: Q6HJ27_BACHK
Original site: Q6HJ27_BACHK 
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
//
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