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Database: UniProt
Entry: Q45563
LinkDB: Q45563
Original site: Q45563 
ID   Q45563_BACSU            Unreviewed;      1274 AA.
AC   Q45563;
DT   01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1996, sequence version 1.
DT   19-JAN-2010, entry version 52.
DE   SubName: Full=Fengycin synthetase;
GN   Name=fenB;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=F29-3;
RX   MEDLINE=95379756; PubMed=7651334; DOI=10.1007/BF02190792;
RA   Chen C.L., Chang L.K., Chang Y.S., Liu S.T., Tschen J.S.;
RT   "Transposon mutagenesis and cloning of the genes encoding the enzymes
RT   of fengycin biosynthesis in Bacillus subtilis.";
RL   Mol. Gen. Genet. 248:121-125(1995).
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DR   EMBL; L42523; AAB00093.1; -; Genomic_DNA.
DR   PDB; 2CB9; X-ray; 1.80 A; A=1043-1274.
DR   PDB; 2CBG; X-ray; 2.50 A; A=1043-1274.
DR   PDBsum; 2CB9; -.
DR   PDBsum; 2CBG; -.
DR   SMR; Q45563; 6-446, 449-956, 889-1039, 953-1266.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR020459; AMP-binding.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Phosphopantetheine.
SQ   SEQUENCE   1274 AA;  143630 MW;  068DA342F321CE95 CRC64;
     MVKTKKIKNV YPLSHMQEGM LFHSFLHKEE GAYVEQSLFT IKGSLSYEIF QRSIQAIIDR
     HDIFRTVFLP HVPNLSGPRQ VVMTERNFHL HTEDISSLQT NEQNDYIEQF KEKDKKKGFD
     LQKDMLMRIS LLKTAENEHV CVWSHHHILM DGWCLGIILQ EFMQIYQSIH TGNHLALEPV
     RPYSTYISWL TKQDKETAAD YWRAYLKNYS TPSQLPRVTD REAKEGYYRE ELIFTLNQKL
     TDKLKETAKQ TGVTLATFIQ TVWGVMLQRY NRTDDVVFGA VVSGRPSEIP GVESMIGLFI
     NTVPVRVKTG KEETFAELLS RCQQDMLDAE PFTCHPLFDI QANTALKQEL IDHIIVFENY
     PLQQKMADSA DQIDSPLQID NVKVSEQSGY NFNLVVAPGD ELVIKFSYNA HVYDAAWMTC
     IQRQLTQALQ AAADHPDIPV ADFSFLDPKE KEQILTQCND TSTAYPKNKT VIDIFREQTV
     KTPDQTALVY GNRSISYREL DQKSDALART LYENGLRRNG TAGILAGHSP EFIISVLAVL
     KAGGTYLPLD AELPPERISY MLSETKAAIL IVQKGLEPNT AFAGTFISAD AEAMIEEHTK
     PLEIVTGPDD LAYIMYTSGS TGRPKGVMIT NRNVVSLVCN SNYTSASVND RFILTGSISF
     DAVTFEMFGA LLKGATLHII DKSTMLTPDR FGAYLIENNI TVLFLTTALF NQLAQAQADM
     FHRLHTLYVG GEALSPELIN AVRRACPNLS LYNIYGPTEN TTFSTFFEIK RDYATPIPIG
     KPISNCTAFI LDAKGCLLPI GVPGELCVGG DGVAKGYLNR DDVTAAVFSP DPFIPGERIY
     RTGDLARWLP DGNLEYISRI DRQIKIRGKR IEPAEIEARL LEIEGVREAA VTLLETDGEV
     QLYTHYVSDE SRNEKEIRAA LARVLPDYMI PQRWVRVDRM PLTGNGKINR SALPVPENES
     ENRQDLTPPR NWVEQELTQI WKSVLGVKTI GIHDDFFALG GHSLKALQVI HMLKHHQHVD
     IPIDVLFENP TIAQLAEKLY SNQLSAAGEQ HVIQLNQQGG KNLFCFPPIS GFGIYFKDLA
     LQLNHKAAVY GFHFIEEDSR IEQYVSRITE IQPEGPYVLL GYSAGGNLAF EVVQAMEQKG
     LEVSDFIIVD AYKKDQSITA DTENDDSAAY LPEAVRETVM QKKRCYQEYW AQLINEGRIK
     SNIHFIEAGI QTETSGAMVL QKWQDAAEEG YAEYTGYGAH KDMLEGEFAE KNANIILNIL
     DKINSDQKVL PNKH
//
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Ontology (6)   
   GO (6)   
Chemical substance (1)   
   KEGG COMPOUND (1)   
DNA sequence (1)   
   EMBL (1)   
3D Structure (2)   
   PDB (2)   
Protein domain (21)   
   InterPro (9)   
   Pfam (4)   
   PROSITE (3)   
   Blocks (4)   
   PRINTS (1)   
Literature (1)   
   PubMed (1)   
All databases (32)   
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