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Protein

Polyketide synthase PksJ

Gene

pksJ

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism.2 Publications

Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 5 phosphopantetheines covalently.Curated

Pathwayi: bacillaene biosynthesis

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei1932 – 19321For beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation
Active sitei3511 – 35111For beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation
Active sitei4743 – 47431For beta-ketoacyl synthase 3 activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Ligase, Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBSUB:BSU17180-MONOMER.
UniPathwayiUPA01003.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyketide synthase PksJ
Short name:
PKS
Gene namesi
Name:pksJ
Synonyms:pksK
Ordered Locus Names:BSU17180
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 50435043Polyketide synthase PksJPRO_0000193184Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei627 – 6271O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei1689 – 16891O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication
Modified residuei3148 – 31481O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei3246 – 32461O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei4496 – 44961O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiP40806.

Interactioni

Protein-protein interaction databases

DIPiDIP-60662N.
IntActiP40806. 7 interactions.
STRINGi224308.Bsubs1_010100009451.

Structurei

Secondary structure

1
5043
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2669 – 267810Combined sources
Beta strandi2692 – 27009Combined sources
Helixi2703 – 271210Combined sources
Turni2713 – 27153Combined sources
Beta strandi2716 – 27216Combined sources
Helixi2728 – 274518Combined sources
Helixi2747 – 27526Combined sources
Beta strandi2755 – 27628Combined sources
Helixi2767 – 27726Combined sources
Helixi2773 – 278311Combined sources
Beta strandi2787 – 279610Combined sources
Turni2797 – 27993Combined sources
Helixi2803 – 28119Combined sources
Beta strandi2818 – 28225Combined sources
Beta strandi2825 – 28339Combined sources
Beta strandi2848 – 28558Combined sources
Turni2856 – 28583Combined sources
Helixi2860 – 287314Combined sources
Beta strandi2877 – 28815Combined sources
Helixi2888 – 289912Combined sources
Beta strandi2903 – 29064Combined sources
Helixi2914 – 292714Combined sources
Beta strandi2933 – 29364Combined sources
Turni2946 – 29483Combined sources
Helixi2951 – 29588Combined sources
Turni2959 – 29624Combined sources
Helixi2963 – 29719Combined sources
Turni2972 – 29743Combined sources
Beta strandi2978 – 29858Combined sources
Helixi2986 – 29905Combined sources
Helixi2996 – 301722Combined sources
Beta strandi3023 – 30308Combined sources
Helixi3044 – 30529Combined sources
Helixi3059 – 307214Combined sources
Beta strandi3075 – 30828Combined sources
Helixi3084 – 30918Combined sources
Beta strandi3342 – 335110Combined sources
Beta strandi3354 – 33563Combined sources
Helixi3357 – 33659Combined sources
Turni3376 – 33783Combined sources
Helixi3381 – 33844Combined sources
Turni3388 – 33903Combined sources
Beta strandi3399 – 34013Combined sources
Beta strandi3406 – 34094Combined sources
Helixi3411 – 34144Combined sources
Helixi3418 – 34214Combined sources
Helixi3426 – 344217Combined sources
Helixi3446 – 34494Combined sources
Beta strandi3455 – 34595Combined sources
Helixi3465 – 34717Combined sources
Helixi3480 – 34845Combined sources
Helixi3489 – 349810Combined sources
Beta strandi3504 – 35074Combined sources
Helixi3510 – 35123Combined sources
Helixi3513 – 352614Combined sources
Beta strandi3531 – 35399Combined sources
Helixi3545 – 35528Combined sources
Beta strandi3577 – 35859Combined sources
Helixi3586 – 35927Combined sources
Beta strandi3597 – 360711Combined sources
Helixi3619 – 363315Combined sources
Helixi3637 – 36393Combined sources
Beta strandi3642 – 36443Combined sources
Helixi3653 – 366917Combined sources
Beta strandi3679 – 36813Combined sources
Beta strandi3684 – 36874Combined sources
Helixi3690 – 36934Combined sources
Helixi3697 – 36993Combined sources
Helixi3700 – 371314Combined sources
Beta strandi3724 – 37263Combined sources
Beta strandi3735 – 37395Combined sources
Beta strandi3752 – 37543Combined sources
Beta strandi3760 – 37667Combined sources
Beta strandi3770 – 37789Combined sources
Beta strandi3795 – 38039Combined sources
Helixi3804 – 381916Combined sources
Helixi3825 – 38273Combined sources
Helixi3828 – 383710Combined sources
Beta strandi3843 – 385210Combined sources
Helixi3853 – 386513Combined sources
Beta strandi3870 – 38778Combined sources
Helixi3878 – 38803Combined sources
Helixi3884 – 38907Combined sources
Helixi3892 – 390312Combined sources
Helixi3907 – 39159Combined sources
Helixi3922 – 39254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4J1QX-ray2.35A2669-3111[»]
4J1SX-ray3.01A2669-3111[»]
4NA1X-ray1.95A/B3336-3951[»]
4NA2X-ray2.30A/B3336-3951[»]
4NA3X-ray2.89A/B3336-3951[»]
ProteinModelPortaliP40806.
SMRiP40806. Positions 29-560, 586-1132, 1135-1645, 1650-1728, 1760-2658, 2736-3096, 3210-3287, 3339-3895, 4052-4419, 4461-4536, 4587-5035.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini591 – 66474Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini1659 – 172668Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST
Domaini3112 – 318574Acyl carrier 3PROSITE-ProRule annotationAdd
BLAST
Domaini3214 – 328370Acyl carrier 4PROSITE-ProRule annotationAdd
BLAST
Domaini4464 – 453370Acyl carrier 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni141 – 481341Adenylation 1Add
BLAST
Regioni690 – 989300CondensationBy similarityAdd
BLAST
Regioni1181 – 1578398Adenylation 2By similarityAdd
BLAST
Regioni1763 – 2189427Beta-ketoacyl synthase 1By similarityAdd
BLAST
Regioni3342 – 3782441Beta-ketoacyl synthase 2By similarityAdd
BLAST
Regioni4591 – 4995405Beta-ketoacyl synthase 3By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili3839 – 387234Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 5 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

eggNOGiENOG4105C0W. Bacteria.
COG0318. LUCA.
COG1020. LUCA.
COG3321. LUCA.
HOGENOMiHOG000008928.
InParanoidiP40806.
KOiK13611.
OMAiEGVGMVM.
OrthoDBiEOG6QP0WP.
PhylomeDBiP40806.

Family and domain databases

Gene3Di1.10.1200.10. 6 hits.
3.40.47.10. 6 hits.
3.40.50.720. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016040. NAD(P)-bd_dom.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00501. AMP-binding. 2 hits.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF16197. KAsynt_C_assoc. 2 hits.
PF00109. ketoacyl-synt. 3 hits.
PF02801. Ketoacyl-synt_C. 3 hits.
PF08659. KR. 2 hits.
PF00550. PP-binding. 5 hits.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00826. PKS_DH. 1 hit.
SM00825. PKS_KS. 3 hits.
SM00823. PKS_PP. 5 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 7 hits.
SSF51735. SSF51735. 3 hits.
SSF53901. SSF53901. 7 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 5 hits.
PS00455. AMP_BINDING. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P40806-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRNNDNIRIL TNPSVSHGEP LHISEKQPAT IPEVLYRTAT ELGDTKGIIY
60 70 80 90 100
LQPDGTEVYQ SYRRLWDDGL RIAKGLRQSG LKAKQSVILQ LGDNSQLLPA
110 120 130 140 150
FWGCVLTGVV PAPLAVPPTY AESSSGTQKL KDAWTLLDKP AVITDRGMHQ
160 170 180 190 200
EMLDWAKEQG LEGFRAIIVE DLLSAEADTD WHQSSPEDLA LLLLTSGSTG
210 220 230 240 250
TPKAVMLNHR NIMSMVKGII QMQGFTREDI TFNWMPFDHV GGIGMLHLRD
260 270 280 290 300
VYLGCQEINV SSETILMEPL KWLDWIDHYR ASVTWAPNFA FGLVTDFAEE
310 320 330 340 350
IKDKKWDLSS MRYMLNGGEA MVAKVGRRIL ELLEPHGLPA DAIRPAWGMS
360 370 380 390 400
ETSSGVIFSH EFTRAGTSDD DHFVEIGSPI PGFSMRIVND HNELVEEGEI
410 420 430 440 450
GRFQVSGLSV TSGYYQRPDL NESVFTEDGW FETGDLGFLR NGRLTITGRT
460 470 480 490 500
KDAIIINGIN YYSHAIESAV EELPEIETSY TAACAVRLGQ NSTDQLAIFF
510 520 530 540 550
VTSAKLNDEQ MSQLLRNIQS HVSQVIGVTP EYLLPVQKEE IPKTAIGKIQ
560 570 580 590 600
RTQLKTSFEN GEFDHLLHKP NRMNDAVQDE GIQQADQVKR VREEIQKHLL
610 620 630 640 650
TCLTEELHVS HDWVEPNANI QSLGVNSIKM MKLIRSIEKN YHIKLTAREI
660 670 680 690 700
HQYPTIERLA SYLSEHEDLS SLSADKKGTD TYKTEPERSQ ATFQPLSEVQ
710 720 730 740 750
KGLWTLQKMS PEKSAYHVPL CFKFSSGLHH ETFQQAFGLV LNQHPILKHV
760 770 780 790 800
IQEKDGVPFL KNEPALSIEI KTENISSLKE SDIPAFLRKK VKEPYVKENS
810 820 830 840 850
PLVRVMSFSR SEQEHFLLVV IHHLIFDGVS SVTFIRSLFD TYQLLLKGQQ
860 870 880 890 900
PEKAVSPAIY HDFAAWEKNM LAGKDGVKHR TYWQKQLSGT LPNLQLPNVS
910 920 930 940 950
ASSVDSQFRE DTYTRRLSSG FMNQVRTFAK EHSVNVTTVF LSCYMMLLGR
960 970 980 990 1000
YTGQKEQIVG MPAMVRPEER FDDAIGHFLN MLPIRSELNP ADTFSSFISK
1010 1020 1030 1040 1050
LQLTILDGLD HAAYPFPKMV RDLNIPRSQA GSPVFQTAFF YQNFLQSGSY
1060 1070 1080 1090 1100
QSLLSRYADF FSVDFVEYIH QEGEYELVFE LWETEEKMEL NIKYNTGLFD
1110 1120 1130 1140 1150
AASISAMFDH FVYVTEQAML NPSQPLKEYS LLPEAEKQMI LKTWNATGKT
1160 1170 1180 1190 1200
YPYITFHELF EQQAKKTPDR AAVSYEGQTL TYRELDEKST QLAIYLQAHG
1210 1220 1230 1240 1250
VGPDRLAGIY VDRSLDMLVG LLAILKAGGA YVPLDPSYPA ERLEYMLEDS
1260 1270 1280 1290 1300
EVFITLTTSE LVNTLSWNGV TTALLDQDWD EIAQTASDRK VLTRTVTPEN
1310 1320 1330 1340 1350
LAYVIYTSGS TGKPKGVMIP HKALTNFLVS MGETPGLTAE DKMLAVTTYC
1360 1370 1380 1390 1400
FDIAALELFL PLIKGAHCYI CQTEHTKDVE KLKRDIRAIK PTVMQATPAT
1410 1420 1430 1440 1450
WKMLFYSGWE NEESVKILCG GEALPETLKR YFLDTGSEAW NMFGPTETTI
1460 1470 1480 1490 1500
WSAVQRINVE CSHATIGRPI ANTQIYITDS QLAPVPAGVP GELCIAGDGV
1510 1520 1530 1540 1550
AKGYYKKEEL TDSRFIDNPF EPGSKLYRTG DMARWLTGGR IEYIGRIDNQ
1560 1570 1580 1590 1600
VKIRGFRIEL GDIESRLSEH PGILECVVVA DMDNLAAYYT AKHANASLTA
1610 1620 1630 1640 1650
RELRHFVKNA LPAYMVPSYF IQLDHMPLTP NGKIDRNSLK NIDLSGEQLK
1660 1670 1680 1690 1700
QRQTSPKNIQ DTVFTIWQEV LKTSDIEWDD GFFDVGGDSL LAVTVADRIK
1710 1720 1730 1740 1750
HELSCEFSVT DLFEYSTIKN ISQYITEQRM GDASDHIPTD PAAHIEDQST
1760 1770 1780 1790 1800
EMSDLPDYYD DSVAIIGISC EFPGAKNHDE FWENLRDGKE SIAFFNKEEL
1810 1820 1830 1840 1850
QRFGISKEIA ENADYVPAKA SIDGKDRFDP SFFQISPKDA EFMDPQLRML
1860 1870 1880 1890 1900
LTHSWKAIED AGYAARQIPQ TSVFMSASNN SYRALLPSDT TESLETPDGY
1910 1920 1930 1940 1950
VSWVLAQSGT IPTMISHKLG LRGPSYFVHA NCSSSLIGLH SAYKSLLSGE
1960 1970 1980 1990 2000
SDYALVGGAT LHTESNIGYV HQPGLNFSSD GHIKAFDASA DGMIGGEGVA
2010 2020 2030 2040 2050
VVLLKKAADA VKDGDHIYAL LRGIGVNNDG ADKVGFYAPS VKGQADVVQQ
2060 2070 2080 2090 2100
VMNQTKVQPE SICYVEAHGT GTKLGDPIEL AALTNVYRQY TNKTQFCGIG
2110 2120 2130 2140 2150
SVKTNIGHLD TAAGLAGCIK VVMSLYHQEL APSVNYKEPN PNTDLASSPF
2160 2170 2180 2190 2200
YVVDQKKTLS REIKTHRAAL SSFGLGGTNT HAIFEQFKRD SDKGKIDGTC
2210 2220 2230 2240 2250
IVPISAKNKE RLQEYAEDIL AYLERRGFEN SQLPDFAYTL QVGREAMEHR
2260 2270 2280 2290 2300
VVFIADHVNE LKQRLTDFIN GNTAIEGCFQ GSKHNAREVS WLTEDEDSAE
2310 2320 2330 2340 2350
LIRKWMAKGK VNKLAEMWSK GAHIDWMQLY KGERPNRMSL PTYPFAKERY
2360 2370 2380 2390 2400
WPSQDDRKPV AQISGNQTGI GSIHPLLHQN TSDFSEQKFS SVFTGDEFFL
2410 2420 2430 2440 2450
RDHVVRGKPV LPGVAYLEMA YAAINQAAGS EIGQDVRIRL NHTVWVQPVV
2460 2470 2480 2490 2500
VDRHSAQVDI SLFPEEDGKI TFDIYSTQED GDDPVIHSQG SAELASAAET
2510 2520 2530 2540 2550
PVADLTEMSR RCGKGKMSPD QFYEEGRSRG MFHGPAFQGI KNVNIGNREV
2560 2570 2580 2590 2600
LAQLQLPEIV SGTNEQFVLH PSIMDSALQT ATICIMQELT DQKLILPFAL
2610 2620 2630 2640 2650
EELEVIKGCS SSMWAYARLS DSDHSGGVVQ KADIDVIDES GTVCVRIKGF
2660 2670 2680 2690 2700
STRVLEGEVH TSKPSTRHER LMLEPVWEKQ NEEREDEDLS YTEHIIVLFE
2710 2720 2730 2740 2750
TERSVTDSIA SHMKDARVIT LNEAVGHIAE RYQCYMQNIF ELLQSKVRKL
2760 2770 2780 2790 2800
SAGRIIIQAI VPLEKEKQLF AGVSGLFKTA EIEFSKLTAQ VIEIEKPEEM
2810 2820 2830 2840 2850
IDLHLKLKDD SRRPFDKQIR YEAGYRFVKG WREMVLPSAD TLHMPWRDEG
2860 2870 2880 2890 2900
VYLITGGAGS LGLLFAKEIA NRTGRSTIVL TGRSVLSEDK ENELEALRSI
2910 2920 2930 2940 2950
GAEVVYREAD VSDQHAVRHL LEEIKERYGT LNGIIHGAGS SKDRFIIHKT
2960 2970 2980 2990 3000
NEEFQEVLQP KVSGLLHVDE CSKDFPLDFF IFFSSVSGCL GNAGQADYAA
3010 3020 3030 3040 3050
ANSFMDAFAE YRRSLAASKK RFGSTISFNW PLWEEGGMQV GAEDEKRMLK
3060 3070 3080 3090 3100
TTGMVPMPTD SGLKAFYQGI VSDKPQVFVM EGQLQKMKQK LLSAGSKAKR
3110 3120 3130 3140 3150
NDQRKADQDQ GQTRKLEAAL IQMVGAILKV NTDDIDVNTE LSEYGFDSVT
3160 3170 3180 3190 3200
FTVFTNKINE KFQLELTPTI FFEYGSVQSL AEYVVAAYQG EWNQDATAKG
3210 3220 3230 3240 3250
KDERTNLVHS LSSLEASLSN MVSAILKVNS EDIDVNTELS EYGFDSVTFT
3260 3270 3280 3290 3300
VFTNKINEEF QLELTPTIFF EYGSLHSLAE YLTVEHGDTL VQEREKPEGQ
3310 3320 3330 3340 3350
EELQTKSSEA PKITSRRKRR FTQPIIAKAE RNKKQAADFE PVAIVGISGR
3360 3370 3380 3390 3400
FPGAMDIDEF WKNLEEGKDS ITEVPKDRWD WREHYGNPDT DVNKTDIKWG
3410 3420 3430 3440 3450
GFIDGVAEFD PLFFGISPRE ADYVDPQQRL LMTYVWKALE DAGCSPQSLS
3460 3470 3480 3490 3500
GTGTGIFIGT GNTGYKDLFH RANLPIEGHA ATGHMIPSVG PNRMSYFLNI
3510 3520 3530 3540 3550
HGPSEPVETA CSSSLVAIHR AVTAMQNGDC EMAIAGGVNT ILTEEAHISY
3560 3570 3580 3590 3600
SKAGMLSTDG RCKTFSADAN GYVRGEGVGM VMLKKLEDAE RDGNHIYGVI
3610 3620 3630 3640 3650
RGTAENHGGR ANTLTSPNPK AQADLLVRAY RQADIDPSTV TYIEAHGTGT
3660 3670 3680 3690 3700
ELGDPIEING LKAAFKELSN MRGESQPDVP DHRCGIGSVK SNIGHLELAA
3710 3720 3730 3740 3750
GISGLIKVLL QMKHKTLVKS LHCETLNPYL QLTDSPFYIV QEKQEWKSVT
3760 3770 3780 3790 3800
DRDGNELPRR AGISSFGIGG VNAHIVIEEY MPKANSEHTA TEQPNVIVLS
3810 3820 3830 3840 3850
AKNKSRLIDR ASQLLEVIRN KKYTDQDLHR IAYTLQVGRE EMDERLACVA
3860 3870 3880 3890 3900
GTMQELEEKL QAFVDGKEET DEFFRGQSHR NKETQTIFTA DEDMALALDA
3910 3920 3930 3940 3950
WIRKRKYAKL ADLWVKGVSI QWNTLYGETK PRLISLPSYP FAKDHYWVPA
3960 3970 3980 3990 4000
KEHSERDKKE LVNAIEDRAA CFLTKQWSLS PIGSAVPGTR TVAILCCQET
4010 4020 4030 4040 4050
ADLAAEVSSY FPNHLLIDVS RIENDQSDID WKEFDGLVDV IGCGWDDEGR
4060 4070 4080 4090 4100
LDWIEWVQRL VEFGHKEGLR LLCVTKGLES FQNTSVRMAG ASRAGLYRML
4110 4120 4130 4140 4150
QCEYSHLISR HMDAEEVTDH RRLAKLIADE FYSDSYDAEV CYRDGLRYQA
4160 4170 4180 4190 4200
FLKAHPETGK ATEQSAVFPK DHVLLITGGT RGIGLLCARH FAECYGVKKL
4210 4220 4230 4240 4250
VLTGREQLPP REEWARFKTS NTSLAEKIQA VRELEAKGVQ VEMLSLTLSD
4260 4270 4280 4290 4300
DAQVEQTLQH IKRTLGPIGG VIHCAGLTDM DTLAFIRKTS DDIQRVLEPK
4310 4320 4330 4340 4350
VSGLTTLYRH VCNEPLQFFV LFSSVSAIIP ELSAGQADYA MANSYMDYFA
4360 4370 4380 4390 4400
EAHQKHAPII SVQWPNWKET GMGEVTNQAY RDSGLLSITN SEGLRFLDQI
4410 4420 4430 4440 4450
VSKKFGPVVL PAMANQTNWE PELLMKRRKP HEGGLQEAAL QSPPARDIEE
4460 4470 4480 4490 4500
ADEVSKCDGL LSETQSWLID LFTEELRIDR EDFEIDGLFQ DYGVDSIILA
4510 4520 4530 4540 4550
QVLQRINRKL EAALDPSILY EYPTIQRFAD WLIGSYSERL SALFGGRISD
4560 4570 4580 4590 4600
ASAPLENKIE AEASVPGKDR ALTPQIQAPA ILSPDSHAEG IAVVGLSCRF
4610 4620 4630 4640 4650
PGAETLESYW SLLSEGRSSI GPIPAERWGC KTPYYAGVID GVSYFDPDFF
4660 4670 4680 4690 4700
LLHEEDVRAM DPQALLVLEE CLKLLYHAGY TPEEIKGKPV GVYIGGRSQH
4710 4720 4730 4740 4750
KPDEDSLDHA KNPIVTVGQN YLAANLSQFF DVRGPSVVVD TACSSALVGM
4760 4770 4780 4790 4800
NMAIQALRGG DIQSAIVGGV SLLSSDASHR LFDRRGILSK HSSFHVFDER
4810 4820 4830 4840 4850
ADGVVLGEGV GMVMLKTVKQ ALEDGDIIYA VVKAASVNND GRTAGPATPN
4860 4870 4880 4890 4900
LEAQKEVMKD ALFKSGKKPE DISYLEANGS GSIVTDLLEL KAIQSVYRSG
4910 4920 4930 4940 4950
HSSPLSLGSI KPNIGHPLCA EGIASFIKVV LMLKERRFVP FLSGEKEMAH
4960 4970 4980 4990 5000
FDQQKANITF SRALEKWTDS QPTAAINCFA DGGTNAHVIV EAWEKDEKHA
5010 5020 5030 5040
IKRSPISPPQ LKKRMLSPGE PKLEAETSKM TAANIWDTYE VEV
Length:5,043
Mass (Da):562,814
Last modified:July 28, 2009 - v3
Checksum:iF6E8A8533D518DE4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti87 – 871V → W in AAA85143 (PubMed:7704258).Curated
Sequence conflicti619 – 6191N → NAN in AAA85144 (PubMed:7704258).Curated
Sequence conflicti4981 – 49811D → G in AAA85144 (PubMed:7704258).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11039 Genomic DNA. Translation: AAA85143.1. Sequence problems.
U11039 Genomic DNA. Translation: AAA85144.1. Sequence problems.
AL009126 Genomic DNA. Translation: CAB13589.3.
PIRiA69679.
H69678.
RefSeqiNP_389598.3. NC_000964.3.
WP_003245563.1. NZ_JNCM01000035.1.

Genome annotation databases

EnsemblBacteriaiCAB13589; CAB13589; BSU17180.
GeneIDi940043.
KEGGibsu:BSU17180.
PATRICi18975245. VBIBacSub10457_1814.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U11039 Genomic DNA. Translation: AAA85143.1. Sequence problems.
U11039 Genomic DNA. Translation: AAA85144.1. Sequence problems.
AL009126 Genomic DNA. Translation: CAB13589.3.
PIRiA69679.
H69678.
RefSeqiNP_389598.3. NC_000964.3.
WP_003245563.1. NZ_JNCM01000035.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4J1QX-ray2.35A2669-3111[»]
4J1SX-ray3.01A2669-3111[»]
4NA1X-ray1.95A/B3336-3951[»]
4NA2X-ray2.30A/B3336-3951[»]
4NA3X-ray2.89A/B3336-3951[»]
ProteinModelPortaliP40806.
SMRiP40806. Positions 29-560, 586-1132, 1135-1645, 1650-1728, 1760-2658, 2736-3096, 3210-3287, 3339-3895, 4052-4419, 4461-4536, 4587-5035.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60662N.
IntActiP40806. 7 interactions.
STRINGi224308.Bsubs1_010100009451.

Proteomic databases

PaxDbiP40806.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13589; CAB13589; BSU17180.
GeneIDi940043.
KEGGibsu:BSU17180.
PATRICi18975245. VBIBacSub10457_1814.

Phylogenomic databases

eggNOGiENOG4105C0W. Bacteria.
COG0318. LUCA.
COG1020. LUCA.
COG3321. LUCA.
HOGENOMiHOG000008928.
InParanoidiP40806.
KOiK13611.
OMAiEGVGMVM.
OrthoDBiEOG6QP0WP.
PhylomeDBiP40806.

Enzyme and pathway databases

UniPathwayiUPA01003.
BioCyciBSUB:BSU17180-MONOMER.

Family and domain databases

Gene3Di1.10.1200.10. 6 hits.
3.40.47.10. 6 hits.
3.40.50.720. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR032821. KAsynt_C_assoc.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016040. NAD(P)-bd_dom.
IPR020841. PKS_Beta-ketoAc_synthase_dom.
IPR020807. PKS_dehydratase.
IPR013968. PKS_KR.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR016039. Thiolase-like.
[Graphical view]
PfamiPF00501. AMP-binding. 2 hits.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF16197. KAsynt_C_assoc. 2 hits.
PF00109. ketoacyl-synt. 3 hits.
PF02801. Ketoacyl-synt_C. 3 hits.
PF08659. KR. 2 hits.
PF00550. PP-binding. 5 hits.
PF14765. PS-DH. 1 hit.
[Graphical view]
SMARTiSM00826. PKS_DH. 1 hit.
SM00825. PKS_KS. 3 hits.
SM00823. PKS_PP. 5 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 7 hits.
SSF51735. SSF51735. 3 hits.
SSF53901. SSF53901. 7 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 5 hits.
PS00455. AMP_BINDING. 2 hits.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence around the 159 degree region of the Bacillus subtilis genome: the pksX locus spans 33.6 kb."
    Albertini A.M., Caramori T., Scoffone F., Scotti C., Galizzi A.
    Microbiology 141:299-309(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / PB1424.
  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 87; 619 AND 4981.
  5. "Activity screening of carrier domains within nonribosomal peptide synthetases using complex substrate mixtures and large molecule mass spectrometry."
    Dorrestein P.C., Blackhall J., Straight P.D., Fischbach M.A., Garneau-Tsodikova S., Edwards D.J., McLaughlin S., Lin M., Gerwick W.H., Kolter R., Walsh C.T., Kelleher N.L.
    Biochemistry 45:1537-1546(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN ACYL CARRIER PROTEIN, PHOSPHOPANTETHEINYLATION AT SER-1689.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  6. Cited for: SUBCELLULAR LOCATION.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  7. "The identification of bacillaene, the product of the PksX megacomplex in Bacillus subtilis."
    Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R., Walsh C.T., Clardy J.
    Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN BACILLAENE BIOSYNTHESIS.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.

Entry informationi

Entry nameiPKSJ_BACSU
AccessioniPrimary (citable) accession number: P40806
Secondary accession number(s): P40803
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 28, 2009
Last modified: May 11, 2016
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The acyl carrier 2 domain binds glycine.

Caution

Was originally thought to be two separate ORFs named pksJ and pksK.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.