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Protein

Dimodular nonribosomal peptide synthase

Gene

dhbF

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Specifically adenylates threonine and glycine, and loads them onto their corresponding peptidyl carrier domains.1 Publication

Cofactori

pantetheine 4'-phosphateBy similarityNote: Binds 1 phosphopantetheine covalently.By similarity

Pathwayi: bacillibactin biosynthesis

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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Enzyme and pathway databases

BioCyciBSUB:BSU31960-MONOMER.
MetaCyc:MONOMER-13921.
UniPathwayiUPA00013.

Protein family/group databases

ESTHERibacsu-YUKL. Thioesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
Dimodular nonribosomal peptide synthase
Gene namesi
Name:dhbF
Ordered Locus Names:BSU31960
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 23782378Dimodular nonribosomal peptide synthasePRO_0000193081Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei996 – 9961O-(pantetheine 4'-phosphoryl)serine1 Publication
Modified residuei2071 – 20711O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiP45745.
PRIDEiP45745.

Interactioni

Protein-protein interaction databases

IntActiP45745. 3 interactions.
MINTiMINT-8364900.
STRINGi224308.Bsubs1_010100017356.

Structurei

3D structure databases

ProteinModelPortaliP45745.
SMRiP45745. Positions 11-953, 956-1492, 1494-2378.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini966 – 103368Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini2041 – 210868Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG1020. LUCA.
COG3319. LUCA.
HOGENOMiHOG000229991.
InParanoidiP45745.
KOiK04780.
OMAiEIECGEQ.
OrthoDBiEOG6XHC08.
PhylomeDBiP45745.

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR009081. PP-bd_ACP.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 2 hits.
PF13193. AMP-binding_C. 2 hits.
PF00668. Condensation. 2 hits.
PF00550. PP-binding. 2 hits.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00823. PKS_PP. 2 hits.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 2 hits.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 2 hits.
PROSITEiPS50075. ACP_DOMAIN. 2 hits.
PS00455. AMP_BINDING. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45745-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDTKDLQYS LTGAQTGIWF AQQLDPDNPI YNTAEYIEIN GPVNIALFEE
60 70 80 90 100
ALRHVIKEAE SLHVRFGENM DGPWQMINPS PDVQLHVIDV SSEPDPEKTA
110 120 130 140 150
LNWMKADLAK PVDLGYAPLF NEALFIAGPD RFFWYQRIHH IAIDGFGFSL
160 170 180 190 200
IAQRVASTYT ALIKGQTAKS RSFGSLQAIL EEDTDYRGSE QYEKDRQFWL
210 220 230 240 250
DRFADAPEVV SLADRAPRTS NSFLRHTAYL PPSDVNALKE AARYFSGSWH
260 270 280 290 300
EVMIAVSAVY VHRMTGSEDV VLGLPMMGRI GSASLNVPAM VMNLLPLRLT
310 320 330 340 350
VSSSMSFSEL IQQISREIRS IRRHHKYRHE ELRRDLKLIG ENHRLFGPQI
360 370 380 390 400
NLMPFDYGLD FAGVRGTTHN LSAGPVDDLS INVYDRTDGS GLRIDVDANP
410 420 430 440 450
EVYSESDIKL HQQRILQLLQ TASAGEDMLI GQMELLLPEE KEKVISKWNE
460 470 480 490 500
TAKSEKLVSL QDMFEKQAVL TPERIALMCD DIQVNYRKLN EEANRLARLL
510 520 530 540 550
IEKGIGPEQF VALALPRSPE MVASMLGVLK TGAAYLPLDP EFPADRISYM
560 570 580 590 600
LEDAKPSCII TTEEIAASLP DDLAVPELVL DQAVTQEIIK RYSPENQDVS
610 620 630 640 650
VSLDHPAYII YTSGSTGRPK GVVVTQKSLS NFLLSMQEAF SLGEEDRLLA
660 670 680 690 700
VTTVAFDISA LELYLPLISG AQIVIAKKET IREPQALAQM IENFDINIMQ
710 720 730 740 750
ATPTLWHALV TSEPEKLRGL RVLVGGEALP SGLLQELQDL HCSVTNLYGP
760 770 780 790 800
TETTIWSAAA FLEEGLKGVP PIGKPIWNTQ VYVLDNGLQP VPPGVVGELY
810 820 830 840 850
IAGTGLARGY FHRPDLTAER FVADPYGPPG TRMYRTGDQA RWRADGSLDY
860 870 880 890 900
IGRADHQIKI RGFRIELGEI DAVLANHPHI EQAAVVVRED QPGDKRLAAY
910 920 930 940 950
VVADAAIDTA ELRRYMGASL PDYMVPSAFV EMDELPLTPN GKLDRKALPA
960 970 980 990 1000
PDFSTSVSDR APRTPQEEIL CDLFAEVLGL ARVGIDDSFF ELGGHSLLAA
1010 1020 1030 1040 1050
RLMSRIREVM GAELGIAKLF DEPTVAGLAA HLDLAQSACP ALQRAERPEK
1060 1070 1080 1090 1100
IPLSFAQRRL WFLHCLEGPS PTYNIPVAVR LSGELDQGLL KAALYDLVCR
1110 1120 1130 1140 1150
HESLRTIFPE SQGTSYQHIL DADRACPELH VTEIAEKELS DRLAEAVRYS
1160 1170 1180 1190 1200
FDLAAEPAFR AELFVIGPDE YVLLLLVHHI VGDGWSLTPL TRDLGTAYAA
1210 1220 1230 1240 1250
RCHGRSPEWA PLAVQYADYA LWQQELLGNE DDPNSLIAGQ LAFWKETLKN
1260 1270 1280 1290 1300
LPDQLELPTD YSRPAEPSHD GDTIHFRIEP EFHKRLQELA RANRVSLFMV
1310 1320 1330 1340 1350
LQSGLAALLT RLGAGTDIPI GSPIAGRNDD ALGDLVGLFI NTLVLRTDTS
1360 1370 1380 1390 1400
GDPSFRELLD RVREVNLAAY DNQDLPFERL VEVLNPARSR ATHPLFQIML
1410 1420 1430 1440 1450
AFQNTPDAEL HLPDMESSLR INSVGSAKFD LTLEISEDRL ADGTPNGMEG
1460 1470 1480 1490 1500
LLEYSTDLFK RETAQALADR LMRLLEAAES DPDEQIGNLD ILAPEEHSSM
1510 1520 1530 1540 1550
VTDWQSVSEK IPHACLPEQF EKQAALRPDA IAVVYENQEL SYAELNERAN
1560 1570 1580 1590 1600
RLARMMISEG VGPEQFVALA LPRSLEMAVG LLAVLKAGAA YLPLDPDYPA
1610 1620 1630 1640 1650
DRIAFMLKDA QPAFIMTNTK AANHIPPVEN VPKIVLDDPE LAEKLNTYPA
1660 1670 1680 1690 1700
GNPKNKDRTQ PLSPLNTAYV IYTSGSTGVP KGVMIPHQNV TRLFAATEHW
1710 1720 1730 1740 1750
FRFSSGDIWT MFHSYAFDFS VWEIWGPLLH GGRLVIVPHH VSRSPEAFLR
1760 1770 1780 1790 1800
LLVKEGVTVL NQTPSAFYQF MQAEREQPDL GQALSLRYVI FGGEALELSR
1810 1820 1830 1840 1850
LEDWYNRHPE NRPQLINMYG ITETTVHVSY IELDRSMAAL RANSLIGCGI
1860 1870 1880 1890 1900
PDLGVYVLDE RLQPVPPGVA GELYVSGAGL ARGYLGRPGL TSERFIADPF
1910 1920 1930 1940 1950
GPPGTRMYRT GDVARLRADG SLDYVGRADH QVKIRGFRIE LGEIEAALVQ
1960 1970 1980 1990 2000
HPQLEDAAVI VREDQPGDKR LAAYVIPSEE TFDTAELRRY AAERLPDYMV
2010 2020 2030 2040 2050
PAAFVTMKEL PLTPNGKLDR KALPAPDFAA AVTGRGPRTP QEEILCDLFM
2060 2070 2080 2090 2100
EVLHLPRVGI DDRFFDLGGH SLLAVQLMSR IREALGVELS IGNLFEAPTV
2110 2120 2130 2140 2150
AGLAERLEMG SSQSALDVLL PLRTSGDKPP LFCVHPAGGL SWCYAGLMTN
2160 2170 2180 2190 2200
IGTDYPIYGL QARGIGQREE LPKTLDDMAA DYIKQIRTVQ PKGPYHLLGW
2210 2220 2230 2240 2250
SLGGNVVQAM ATQLQNQGEE VSLLVMLDAY PNHFLPIKEA PDDEEALIAL
2260 2270 2280 2290 2300
LALGGYDPDS LGEKPLDFEA AIEILRRDGS ALASLDETVI LNLKNTYVNS
2310 2320 2330 2340 2350
VGILGSYKPK TFRGNVLFFR STIIPEWFDP IEPDSWKPYI NGQIEQIDID
2360 2370
CRHKDLCQPE PLAQIGKVLA VKLEELNK
Length:2,378
Mass (Da):263,770
Last modified:July 28, 2009 - v4
Checksum:i80216ABF9D6BFA66
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2141 – 21411S → G in AAD56240 (PubMed:11112781).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF184977 Genomic DNA. Translation: AAD56240.1.
AL009126 Genomic DNA. Translation: CAB15186.3.
U26444 Genomic DNA. Translation: AAC44634.1.
PIRiE69615.
RefSeqiNP_391076.3. NC_000964.3.
WP_009968094.1. NZ_JNCM01000033.1.

Genome annotation databases

EnsemblBacteriaiCAB15186; CAB15186; BSU31960.
GeneIDi936569.
KEGGibsu:BSU31960.
PATRICi18978364. VBIBacSub10457_3345.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF184977 Genomic DNA. Translation: AAD56240.1.
AL009126 Genomic DNA. Translation: CAB15186.3.
U26444 Genomic DNA. Translation: AAC44634.1.
PIRiE69615.
RefSeqiNP_391076.3. NC_000964.3.
WP_009968094.1. NZ_JNCM01000033.1.

3D structure databases

ProteinModelPortaliP45745.
SMRiP45745. Positions 11-953, 956-1492, 1494-2378.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP45745. 3 interactions.
MINTiMINT-8364900.
STRINGi224308.Bsubs1_010100017356.

Protein family/group databases

ESTHERibacsu-YUKL. Thioesterase.

Proteomic databases

PaxDbiP45745.
PRIDEiP45745.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB15186; CAB15186; BSU31960.
GeneIDi936569.
KEGGibsu:BSU31960.
PATRICi18978364. VBIBacSub10457_3345.

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG1020. LUCA.
COG3319. LUCA.
HOGENOMiHOG000229991.
InParanoidiP45745.
KOiK04780.
OMAiEIECGEQ.
OrthoDBiEOG6XHC08.
PhylomeDBiP45745.

Enzyme and pathway databases

UniPathwayiUPA00013.
BioCyciBSUB:BSU31960-MONOMER.
MetaCyc:MONOMER-13921.

Family and domain databases

Gene3Di1.10.1200.10. 2 hits.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR009081. PP-bd_ACP.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 2 hits.
PF13193. AMP-binding_C. 2 hits.
PF00668. Condensation. 2 hits.
PF00550. PP-binding. 2 hits.
PF00975. Thioesterase. 1 hit.
[Graphical view]
SMARTiSM00823. PKS_PP. 2 hits.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 2 hits.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 2 hits.
PROSITEiPS50075. ACP_DOMAIN. 2 hits.
PS00455. AMP_BINDING. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin."
    May J.J., Wendrich T.M., Marahiel M.A.
    J. Biol. Chem. 276:7209-7217(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
    Strain: 168.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.
  3. "Detecting and analyzing DNA sequencing errors: toward a higher quality of the Bacillus subtilis genome sequence."
    Medigue C., Rose M., Viari A., Danchin A.
    Genome Res. 9:1116-1127(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
    Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
    Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION TO 2141.
  5. "Duplicate isochorismate synthase genes of Bacillus subtilis: regulation and involvement in the biosyntheses of menaquinone and 2,3-dihydroxybenzoate."
    Rowland B.M., Taber H.W.
    J. Bacteriol. 178:854-861(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-95.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  6. "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis."
    Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M.
    Mol. Cell. Proteomics 6:697-707(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHOPANTETHEINYLATION [LARGE SCALE ANALYSIS] AT SER-996, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: 168.

Entry informationi

Entry nameiDHBF_BACSU
AccessioniPrimary (citable) accession number: P45745
Secondary accession number(s): Q9R9I2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 28, 2009
Last modified: May 11, 2016
This is version 130 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

The phosphoserine observed at Ser-996 in PubMed:17218307 undoubtedly results from the secondary neutral loss of pantetheine from the phosphodiester linked cofactor.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.