ID   BACB_BACLI              Reviewed;        2607 AA.
AC   O68007;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   15-DEC-2009, entry version 64.
DE   RecName: Full=Bacitracin synthetase 2;
DE            Short=BA2;
DE   Includes:
DE     RecName: Full=ATP-dependent lysine adenylase;
DE              Short=LysA;
DE     AltName: Full=Lysine activase;
DE   Includes:
DE     RecName: Full=ATP-dependent D-ornithine adenylase;
DE              Short=D-OrnA;
DE     AltName: Full=D-ornithine activase;
DE   Includes:
DE     RecName: Full=Ornithine racemase;
DE              EC=5.1.1.12;
GN   Name=bacB;
OS   Bacillus licheniformis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10716 / NCIB 8874 / IFO 12199;
RX   MEDLINE=98089193; PubMed=9427658; DOI=10.1016/S1074-5521(97)90301-X;
RA   Konz D., Klens A., Schoergendorfer K., Marahiel M.A.;
RT   "The bacitracin biosynthesis operon of Bacillus licheniformis ATCC
RT   10716: molecular characterization of three multi-modular peptide
RT   synthetases.";
RL   Chem. Biol. 4:927-937(1997).
CC   -!- FUNCTION: Activates two amino acids and incorporate a D-ornithine
CC       from its second active site into bacitracin.
CC   -!- CATALYTIC ACTIVITY: L-ornithine = D-ornithine.
CC   -!- COFACTOR: Binds 2 phosphopantetheines covalently (Potential).
CC   -!- PATHWAY: Antibiotic biosynthesis; bacitracin biosynthesis.
CC   -!- SUBUNIT: Large multienzyme complex of BA1, BA2 and BA3.
CC   -!- DOMAIN: Consists of two modules with a C-terminal epimerization
CC       domain. Each module incorporates one amino acid into the peptide
CC       product and can be further subdivided into domains responsible for
CC       substrate adenylation, thiolation, condensation (not for the
CC       initiation module), and epimerization (optional), and N
CC       methylation (optional).
CC   -!- MISCELLANEOUS: Bacitracin is a mixture of at least ten cyclic
CC       dodecapeptides, that differ by one or two amino acids. The most
CC       abundant is bacitracin A, a branched cyclic dodecapeptide. It
CC       contains an N-terminal linear pentapeptide moiety (Ile-Cys-Leu-D-
CC       Glu-Ile) with an isoleucine-cysteine thiazoline condensation
CC       product and a C-terminal heptapeptide ring (Lys-D-Orn-Ile-D-Phe-
CC       His-D-Asp-Asn), in which the free alpha-carboxy group of the C-
CC       terminal Asn is bound to the epsilon-amino group of Lys.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC       family.
CC   -!- SIMILARITY: Contains 2 acyl carrier domains.
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DR   EMBL; AF007865; AAC06347.1; -; Genomic_DNA.
DR   PIR; T31678; T31678.
DR   BRENDA; 5.1.1.12; 1017.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:InterPro.
DR   GO; GO:0048037; F:cofactor binding; IEA:InterPro.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0050157; F:ornithine racemase activity; IEA:EC.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR009081; Acyl_carrier_prot-like.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR006163; Phsphopanteth_bd.
DR   InterPro; IPR006162; PPantetheine_attach_site.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF00668; Condensation; 3.
DR   Pfam; PF00550; PP-binding; 2.
DR   PROSITE; PS50075; ACP_DOMAIN; 2.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis; Isomerase; Ligase; Multifunctional enzyme;
KW   Phosphopantetheine; Repeat.
FT   CHAIN         1   2607       Bacitracin synthetase 2.
FT                                /FTId=PRO_0000193083.
FT   DOMAIN     1021   1088       Acyl carrier 1.
FT   DOMAIN     2064   2130       Acyl carrier 2.
FT   REGION      535   1090       Domain 1 (lysine-activating).
FT   REGION     1547   2141       Domain 2 (D-ornithine-activating).
FT   MOD_RES    1051   1051       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
FT   MOD_RES    2094   2094       O-(pantetheine 4'-phosphoryl)serine (By
FT                                similarity).
SQ   SEQUENCE   2607 AA;  297479 MW;  FF654FAC5B8BBA6F CRC64;
     MSMSIMDFIN DLKKKNITLY HNKGKIKIIG PQELLTADLK QQIKRYKEDI IAALEAGETD
     IERSFPKAAP SKSGTYPLSR EQKRMFILNQ LDDSKTAYNM PLAVKINGEV QISRLEQAWK
     ALIKRHESLR TSFVMLDGEP VQKIEQEAEF RLEYSELGDQ SIQEKISRFI KPFELEKAPL
     LRAEIVKVDE AEHMMMVDMH HIISDGVSIG ILMKEFADCC EGKELSPLAV QYKDYSEWQR
     DIEQQSRLKK QEAYWLNTFR GDIPVLNMPL DFPRPKIRSF QGNRTVVELD QDTTKKLKTI
     AAKNGVTMYM LLLAGYTILL SKYTGQEDII VGSPIAGRPH ADLNGTIGMF VGTLALRNRP
     KGNMTFSEYV QTVKNNTLKA YENQDYQFDA LIEHLGLTHD MSRNPLFDTM FDLQHADDFA
     SEAGGGHFET YDIPFHVAKF DVSLTAFLHG DNLKFDFQYC TDLYKKETVE RMAGHFLNVL
     KDAAHHPELA LSEIRMMSEE EKDIILHTFN HEKTDGPKNK TLSRLFEERA EKTPDHTAVI
     FEDQQLTYRE LNEKANQLAW LLREKGVKPD TIVAIMTDRS LEMIIGIIGI LKAGGAYLPI
     DPDYPEDRVK YMLEDSGADM VVIQEPFKSK IDGRQLITAE DTRSFSKENL PNVNKASDLA
     YVIYTSGSSG RPKGVMTTHR NVVHYVDAFT KRIPLSEHDT VLQVVSFSFD AFSEEVYPIL
     ACSGRLVISR KVSDLNIDEL VKTIGKYRVT LVSCSPLLLN EIDKNQHLTF HPQMKFISGG
     DVLKFEYVEN IIKGADVYNS YGPTEATVCA TYYQLSSADR KKTSIPIGKP LSNYKVYIAD
     QYGRPQPVGV PGELLIGGEG VARGYLNHET LTKAAFVVDE SGERVYRTGD LARWLSDGNI
     EFLGRIDSQV KIRGYRIELE EIEHRLLMND NINEAIVVAK EDQENSKYLC AYIAFNNKNA
     DIEQVQERLA KDLPEYMIPS CFIKLDQIPR TINGKADLKA LPEPDRRAFA QARYEAPRNQ
     TEALLLSIWQ DILPAEQIGI NDHFFDIGGH SLKAFSMAAK IQSALKVEVT LKEIFNHSTI
     QDLAAYIAQK QKQVQSDIQK AEKKEYYPLS SAQKRLYILN QIEEGQTAYN MPFAMKIKGE
     LQTDKAEKAF RTLIKRHESS RTSFVTINGE PVQNINEEVT FEMKYRELDN CSLRERMNQF
     IRPFELEKAP LLRAELVRVN AAEHILLLDM HHIISDGVSI GILMKEWAAL YEEKELAPLK
     IQYKDYSEWQ RDPWQKDRLK KQEESWLSVF QNDIPVLNMP TDFPRPQMQS YEGDRIAFAI
     ERELTDKLKK TAKENGVTMY MLLLAGYTIL LSKYTGQEDI IVGSPIAGRT REELEQTVGM
     FVGTLAMRNH PKGGRTFIEY LQDVKENTFN AYENQDYPFD ELVDKLDLER DISRNALFDT
     MFDMQALDDA EPDIEGLHVE PVDLEFQISK FDLSLTAAES AGVITFHLEF CTRLYKKETA
     ETLAQHFVNI LRDISDHPQK TLNDISMLSE EERHTVLYQF NDTNTEHPSG IFSELFEEQA
     EKSPNHPAAV FKDQMLTYRE LNEKANQLAR TLRQKGVQRE SVVGIMAERS LEMLTGILAV
     LKAGGAYMPI DPGLPKERIQ YLITDSGADL LLTQHQLIGS ISFAGEIIQI DQADAYDTDG
     SNLEHLNSPG DLAYVIYTSG TTGNPKGVMV EHRNIIHAHY TWRKHYELAS FSVNLLQLAS
     MSFDVFAGDL CRSLLNGGTM YIVPDDVKLE MNLLYDMINK YGIHMLESTP SLIIPLMKYI
     DHHKLDFSSM KLLIMGSDTC TIKDYKWLVE RFGQRMRIIN SYGVTEASVD SGYYEEALDR
     IPEIANTPIG KPLDNTAFYI LDPSLNPQPV GVYGELYIGG EGIARGYLNK PELTKERFVP
     NRFAAGGNMY KTGDLARWLP DGNVEFLGRI DHQVKIRGFR IETGEIETKL LENQNISEAV
     VIDREDKKGH KYLCAYIVAR AKTNTNELRE YLSDHLPDYM LPSYFIQINK MPLTPNGKID
     RKALPEPAGD VIAASGYEAP RNETEEKLAA VWQEVLDRDK IGINDNFFEI GGDSIKALQI
     VSKLSRADLK LQVKDLFTNP FIRHLSKYVK KETKARTSEI VQGQVPLTPV QRSFFEANQR
     EQNHYNQAFM LYRENGFAER IVEKVFRKLT EHHDALRMVY WEKNGDIIQH NRGLEDSVFD
     LYVYDLKTEK NLEKTVYQIA TNIQKDISIS EGKMIKLCVF KTTEGDHLLI AIHHLLVDGV
     SWRILFEDFE AAYGQALQGK PIELGYKTDS YKTFSEKLAE YANSKKLLKE QEYWREISKG
     KMAFLPKHRQ AAHDNYENSR TLRISLSQTE TEQLLKEAHK AYNTQINDLL LTALLIASRQ
     LTGENRLKIL MEGHGRDDIL QDVDITRTVG WFTAMYPVFI DLEDEADLSV MIKIVKETLR
     KIPNNGIGYG ILKYLRKDEG LLKDEKPPIL FNYLGELDHD LTTEQFSSSK LSAGQSIGEK
     SARDASVEID SVVAGRQLMI STTFNEYEYS PDTISELNQA FKESLQMVIS HCTGKHETEK
     TSSDYGYDKL SLEDLEELLN EYESVDS
//