BACB_BACLI
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 03-AUG-2022, entry version 103.
DE RecName: Full=Bacitracin synthase 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; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10716 / DSM 603 / NBRC 12199 / NCIMB 8874 / Tracy I;
RX 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 10716:
RT molecular characterization of three multi-modular peptide synthetases.";
RL Chem. Biol. 4:927-937(1997).
CC -!- FUNCTION: Activates two amino acids and incorporate a D-ornithine from
CC its second active site into bacitracin.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine = D-ornithine; Xref=Rhea:RHEA:11584,
CC ChEBI:CHEBI:46911, ChEBI:CHEBI:57668; EC=5.1.1.12;
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};
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 domain.
CC Each module incorporates one amino acid into the peptide product and
CC can be further subdivided into domains responsible for substrate
CC adenylation, thiolation, condensation (not for the initiation module),
CC and epimerization (optional), and N 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 contains
CC an N-terminal linear pentapeptide moiety (Ile-Cys-Leu-D-Glu-Ile) with
CC an isoleucine-cysteine thiazoline condensation product and a C-terminal
CC heptapeptide ring (Lys-D-Orn-Ile-D-Phe-His-D-Asp-Asn), in which the
CC free alpha-carboxy group of the C-terminal Asn is bound to the epsilon-
CC amino group of Lys.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF007865; AAC06347.1; -; Genomic_DNA.
DR PIR; T31678; T31678.
DR AlphaFoldDB; O68007; -.
DR SMR; O68007; -.
DR PRIDE; O68007; -.
DR UniPathway; UPA00179; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0050157; F:ornithine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.10.1830; -; 1.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 3.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR010060; NRPS_synth.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR041464; TubC_N.
DR InterPro; IPR044894; TubC_N_sf.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF18563; TubC_N; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Isomerase; Ligase; Multifunctional enzyme;
KW Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..2607
FT /note="Bacitracin synthase 2"
FT /id="PRO_0000193083"
FT DOMAIN 1016..1091
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2059..2133
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 535..1090
FT /note="Domain 1 (lysine-activating)"
FT REGION 1547..2141
FT /note="Domain 2 (D-ornithine-activating)"
FT MOD_RES 1051
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2094
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
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
