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Protein

Bacitracin synthase 2

Gene

bacB

Organism
Bacillus licheniformis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Activates two amino acids and incorporate a D-ornithine from its second active site into bacitracin.

Catalytic activityi

L-ornithine = D-ornithine.

Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 2 phosphopantetheines covalently.Curated

Pathwayi: bacitracin biosynthesis

This protein is involved in the pathway bacitracin biosynthesis, which is part of Antibiotic biosynthesis.
View all proteins of this organism that are known to be involved in the pathway bacitracin biosynthesis and in Antibiotic biosynthesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Ligase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00179.

Names & Taxonomyi

Protein namesi
Recommended name:
Bacitracin synthase 2
Short name:
BA2
Including the following 3 domains:
ATP-dependent lysine adenylase
Short name:
LysA
Alternative name(s):
Lysine activase
ATP-dependent D-ornithine adenylase
Short name:
D-OrnA
Alternative name(s):
D-ornithine activase
Ornithine racemase (EC:5.1.1.12)
Gene namesi
Name:bacB
OrganismiBacillus licheniformis
Taxonomic identifieri1402 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001930831 – 2607Bacitracin synthase 2Add BLAST2607

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1051O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1
Modified residuei2094O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PRIDEiO68007.

Interactioni

Subunit structurei

Large multienzyme complex of BA1, BA2 and BA3.

Structurei

3D structure databases

ProteinModelPortaliO68007.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1021 – 1088Acyl carrier 1PROSITE-ProRule annotationAdd BLAST68
Domaini2064 – 2130Acyl carrier 2PROSITE-ProRule annotationAdd BLAST67

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni535 – 1090Domain 1 (lysine-activating)Add BLAST556
Regioni1547 – 2141Domain 2 (D-ornithine-activating)Add BLAST595

Domaini

Consists of two modules with a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional), and N methylation (optional).

Sequence similaritiesi

Contains 2 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00501. AMP-binding. 2 hits.
PF13193. AMP-binding_C. 2 hits.
PF00668. Condensation. 3 hits.
PF00550. PP-binding. 2 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 2 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 2 hits.
TIGR01720. NRPS-para261. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 2 hits.
PS00455. AMP_BINDING. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O68007-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSMSIMDFIN DLKKKNITLY HNKGKIKIIG PQELLTADLK QQIKRYKEDI
60 70 80 90 100
IAALEAGETD IERSFPKAAP SKSGTYPLSR EQKRMFILNQ LDDSKTAYNM
110 120 130 140 150
PLAVKINGEV QISRLEQAWK ALIKRHESLR TSFVMLDGEP VQKIEQEAEF
160 170 180 190 200
RLEYSELGDQ SIQEKISRFI KPFELEKAPL LRAEIVKVDE AEHMMMVDMH
210 220 230 240 250
HIISDGVSIG ILMKEFADCC EGKELSPLAV QYKDYSEWQR DIEQQSRLKK
260 270 280 290 300
QEAYWLNTFR GDIPVLNMPL DFPRPKIRSF QGNRTVVELD QDTTKKLKTI
310 320 330 340 350
AAKNGVTMYM LLLAGYTILL SKYTGQEDII VGSPIAGRPH ADLNGTIGMF
360 370 380 390 400
VGTLALRNRP KGNMTFSEYV QTVKNNTLKA YENQDYQFDA LIEHLGLTHD
410 420 430 440 450
MSRNPLFDTM FDLQHADDFA SEAGGGHFET YDIPFHVAKF DVSLTAFLHG
460 470 480 490 500
DNLKFDFQYC TDLYKKETVE RMAGHFLNVL KDAAHHPELA LSEIRMMSEE
510 520 530 540 550
EKDIILHTFN HEKTDGPKNK TLSRLFEERA EKTPDHTAVI FEDQQLTYRE
560 570 580 590 600
LNEKANQLAW LLREKGVKPD TIVAIMTDRS LEMIIGIIGI LKAGGAYLPI
610 620 630 640 650
DPDYPEDRVK YMLEDSGADM VVIQEPFKSK IDGRQLITAE DTRSFSKENL
660 670 680 690 700
PNVNKASDLA YVIYTSGSSG RPKGVMTTHR NVVHYVDAFT KRIPLSEHDT
710 720 730 740 750
VLQVVSFSFD AFSEEVYPIL ACSGRLVISR KVSDLNIDEL VKTIGKYRVT
760 770 780 790 800
LVSCSPLLLN EIDKNQHLTF HPQMKFISGG DVLKFEYVEN IIKGADVYNS
810 820 830 840 850
YGPTEATVCA TYYQLSSADR KKTSIPIGKP LSNYKVYIAD QYGRPQPVGV
860 870 880 890 900
PGELLIGGEG VARGYLNHET LTKAAFVVDE SGERVYRTGD LARWLSDGNI
910 920 930 940 950
EFLGRIDSQV KIRGYRIELE EIEHRLLMND NINEAIVVAK EDQENSKYLC
960 970 980 990 1000
AYIAFNNKNA DIEQVQERLA KDLPEYMIPS CFIKLDQIPR TINGKADLKA
1010 1020 1030 1040 1050
LPEPDRRAFA QARYEAPRNQ TEALLLSIWQ DILPAEQIGI NDHFFDIGGH
1060 1070 1080 1090 1100
SLKAFSMAAK IQSALKVEVT LKEIFNHSTI QDLAAYIAQK QKQVQSDIQK
1110 1120 1130 1140 1150
AEKKEYYPLS SAQKRLYILN QIEEGQTAYN MPFAMKIKGE LQTDKAEKAF
1160 1170 1180 1190 1200
RTLIKRHESS RTSFVTINGE PVQNINEEVT FEMKYRELDN CSLRERMNQF
1210 1220 1230 1240 1250
IRPFELEKAP LLRAELVRVN AAEHILLLDM HHIISDGVSI GILMKEWAAL
1260 1270 1280 1290 1300
YEEKELAPLK IQYKDYSEWQ RDPWQKDRLK KQEESWLSVF QNDIPVLNMP
1310 1320 1330 1340 1350
TDFPRPQMQS YEGDRIAFAI ERELTDKLKK TAKENGVTMY MLLLAGYTIL
1360 1370 1380 1390 1400
LSKYTGQEDI IVGSPIAGRT REELEQTVGM FVGTLAMRNH PKGGRTFIEY
1410 1420 1430 1440 1450
LQDVKENTFN AYENQDYPFD ELVDKLDLER DISRNALFDT MFDMQALDDA
1460 1470 1480 1490 1500
EPDIEGLHVE PVDLEFQISK FDLSLTAAES AGVITFHLEF CTRLYKKETA
1510 1520 1530 1540 1550
ETLAQHFVNI LRDISDHPQK TLNDISMLSE EERHTVLYQF NDTNTEHPSG
1560 1570 1580 1590 1600
IFSELFEEQA EKSPNHPAAV FKDQMLTYRE LNEKANQLAR TLRQKGVQRE
1610 1620 1630 1640 1650
SVVGIMAERS LEMLTGILAV LKAGGAYMPI DPGLPKERIQ YLITDSGADL
1660 1670 1680 1690 1700
LLTQHQLIGS ISFAGEIIQI DQADAYDTDG SNLEHLNSPG DLAYVIYTSG
1710 1720 1730 1740 1750
TTGNPKGVMV EHRNIIHAHY TWRKHYELAS FSVNLLQLAS MSFDVFAGDL
1760 1770 1780 1790 1800
CRSLLNGGTM YIVPDDVKLE MNLLYDMINK YGIHMLESTP SLIIPLMKYI
1810 1820 1830 1840 1850
DHHKLDFSSM KLLIMGSDTC TIKDYKWLVE RFGQRMRIIN SYGVTEASVD
1860 1870 1880 1890 1900
SGYYEEALDR IPEIANTPIG KPLDNTAFYI LDPSLNPQPV GVYGELYIGG
1910 1920 1930 1940 1950
EGIARGYLNK PELTKERFVP NRFAAGGNMY KTGDLARWLP DGNVEFLGRI
1960 1970 1980 1990 2000
DHQVKIRGFR IETGEIETKL LENQNISEAV VIDREDKKGH KYLCAYIVAR
2010 2020 2030 2040 2050
AKTNTNELRE YLSDHLPDYM LPSYFIQINK MPLTPNGKID RKALPEPAGD
2060 2070 2080 2090 2100
VIAASGYEAP RNETEEKLAA VWQEVLDRDK IGINDNFFEI GGDSIKALQI
2110 2120 2130 2140 2150
VSKLSRADLK LQVKDLFTNP FIRHLSKYVK KETKARTSEI VQGQVPLTPV
2160 2170 2180 2190 2200
QRSFFEANQR EQNHYNQAFM LYRENGFAER IVEKVFRKLT EHHDALRMVY
2210 2220 2230 2240 2250
WEKNGDIIQH NRGLEDSVFD LYVYDLKTEK NLEKTVYQIA TNIQKDISIS
2260 2270 2280 2290 2300
EGKMIKLCVF KTTEGDHLLI AIHHLLVDGV SWRILFEDFE AAYGQALQGK
2310 2320 2330 2340 2350
PIELGYKTDS YKTFSEKLAE YANSKKLLKE QEYWREISKG KMAFLPKHRQ
2360 2370 2380 2390 2400
AAHDNYENSR TLRISLSQTE TEQLLKEAHK AYNTQINDLL LTALLIASRQ
2410 2420 2430 2440 2450
LTGENRLKIL MEGHGRDDIL QDVDITRTVG WFTAMYPVFI DLEDEADLSV
2460 2470 2480 2490 2500
MIKIVKETLR KIPNNGIGYG ILKYLRKDEG LLKDEKPPIL FNYLGELDHD
2510 2520 2530 2540 2550
LTTEQFSSSK LSAGQSIGEK SARDASVEID SVVAGRQLMI STTFNEYEYS
2560 2570 2580 2590 2600
PDTISELNQA FKESLQMVIS HCTGKHETEK TSSDYGYDKL SLEDLEELLN

EYESVDS
Length:2,607
Mass (Da):297,479
Last modified:August 1, 1998 - v1
Checksum:iFF654FAC5B8BBA6F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007865 Genomic DNA. Translation: AAC06347.1.
PIRiT31678.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF007865 Genomic DNA. Translation: AAC06347.1.
PIRiT31678.

3D structure databases

ProteinModelPortaliO68007.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiO68007.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00179.

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00501. AMP-binding. 2 hits.
PF13193. AMP-binding_C. 2 hits.
PF00668. Condensation. 3 hits.
PF00550. PP-binding. 2 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 2 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 2 hits.
TIGR01720. NRPS-para261. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 2 hits.
PS00455. AMP_BINDING. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiBACB_BACLI
AccessioniPrimary (citable) accession number: O68007
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: August 1, 1998
Last modified: October 5, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Bacitracin is a mixture of at least ten cyclic dodecapeptides, that differ by one or two amino acids. The most abundant is bacitracin A, a branched cyclic dodecapeptide. It contains an N-terminal linear pentapeptide moiety (Ile-Cys-Leu-D-Glu-Ile) with an isoleucine-cysteine thiazoline condensation product and a C-terminal heptapeptide ring (Lys-D-Orn-Ile-D-Phe-His-D-Asp-Asn), in which the free alpha-carboxy group of the C-terminal Asn is bound to the epsilon-amino group of Lys.

Keywords - Technical termi

Multifunctional enzyme

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.