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Protein

Polyketide synthase PksN

Gene

pksN

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 3 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 sitei1261 – 12611For beta-ketoacyl synthase 1 activityPROSITE-ProRule annotation
Active sitei2747 – 27471For beta-ketoacyl synthase 2 activityPROSITE-ProRule annotation
Active sitei4245 – 42451For beta-ketoacyl synthase 3 activityPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Ligase, Transferase

Keywords - Ligandi

NADP

Enzyme and pathway databases

BioCyciBSUB:BSU17210-MONOMER.
UniPathwayiUPA01003.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyketide synthase PksN (EC:2.3.1.-)
Gene namesi
Name:pksN
Ordered Locus Names:BSU17210
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 – 54885488Polyketide synthase PksNPRO_0000379566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1018 – 10181O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation1 Publication
Modified residuei2485 – 24851O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei3986 – 39861O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiO31782.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009466.

Structurei

3D structure databases

ProteinModelPortaliO31782.
SMRiO31782. Positions 3-443, 445-973, 979-1057, 1089-1989, 2064-2424, 2454-2523, 2575-3488, 3565-3924, 3954-4024, 4075-4984, 5299-5377.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati165 – 20541WD 1Add
BLAST
Repeati965 – 100642WD 2Add
BLAST
Domaini988 – 105568Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Repeati2165 – 220440WD 3Add
BLAST
Domaini2449 – 252274Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST
Repeati3666 – 370540WD 4Add
BLAST
Domaini3950 – 402374Acyl carrier 3PROSITE-ProRule annotationAdd
BLAST
Repeati5206 – 524439WD 5Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni3 – 301299CondensationAdd
BLAST
Regioni493 – 903411AdenylationAdd
BLAST
Regioni1092 – 1518427Beta-ketoacyl synthase 1Add
BLAST
Regioni2579 – 3015437Beta-ketoacyl synthase 2Add
BLAST
Regioni4079 – 4514436Beta-ketoacyl synthase 3Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili3038 – 310972Sequence analysisAdd
BLAST
Coiled coili3626 – 365530Sequence analysisAdd
BLAST
Coiled coili5275 – 530329Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1176 – 11816Poly-Leu

Sequence similaritiesi

Contains 3 acyl carrier domains.PROSITE-ProRule annotation
Contains 5 WD repeats.Curated

Keywords - Domaini

Coiled coil, Repeat, WD repeat

Phylogenomic databases

eggNOGiENOG4105C0W. Bacteria.
COG1020. LUCA.
HOGENOMiHOG000008929.
InParanoidiO31782.
KOiK13614.
OMAiGPNRVSY.
OrthoDBiEOG6QP0WP.
PhylomeDBiO31782.

Family and domain databases

Gene3Di1.10.1200.10. 5 hits.
3.10.129.10. 1 hit.
3.40.47.10. 6 hits.
3.40.50.720. 3 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR029069. HotDog_dom.
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. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF16197. KAsynt_C_assoc. 3 hits.
PF00109. ketoacyl-synt. 3 hits.
PF02801. Ketoacyl-synt_C. 3 hits.
PF08659. KR. 3 hits.
PF00550. PP-binding. 3 hits.
PF14765. PS-DH. 3 hits.
[Graphical view]
SMARTiSM00826. PKS_DH. 3 hits.
SM00825. PKS_KS. 3 hits.
SM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 5 hits.
SSF51735. SSF51735. 4 hits.
SSF53901. SSF53901. 7 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31782-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRQLKSPLS EGQKGLWMLQ KMSPGMSAYN IPLCFRFSKP IHAETFKKAL
60 70 80 90 100
LFVQRQYPVL ASVIQEENGI PFQSVQLSKD LYFVEEDISA MKSADIMPFL
110 120 130 140 150
KEKAKEPFQL EAGPLWRTHL FHRLEECIVL ITIHHIIFDG VSMLTLISAL
160 170 180 190 200
FEAYQQLLNG IEPLQQPSTA DYYDFVDWEN RMLTGREGEE HLAYWKEQLS
210 220 230 240 250
GSLPVLDLPA DRPRSSARKF KGQAYKSLLP HHLRNQIKSF ARTNHVNESV
260 270 280 290 300
VFLSIYKVLL HHYTKQKDII VGVPTMGRQE DRFETLIGYF INMMAVRSKN
310 320 330 340 350
IGSQPLTAFI RELQLTVAVG LDHAAFPFPA LVRELNVDRS AADSPVFQTA
360 370 380 390 400
FLYQNFFQAT GLQKVLEPYQ TLGIEYIEDI RQEGEFELAL EIYEQENETV
410 420 430 440 450
LHLLYNPDLY ELSSIESMME NYMKLAQHMM EDPSLPLEAY SLQLNQEQTS
460 470 480 490 500
LLEQWNATGT NIANDKCIHE VFEEKAKQTP DAVAVMFEDR SLTYKEVDEK
510 520 530 540 550
STSVAVYLQH QGVRPEQPVG ICAERSFDMI IGILGILKAG GAYVPLDPSF
560 570 580 590 600
PQERLKYMLK DSQASIVLTQ PNVHDRISGL TGSHVKAINI ELACRNGYTD
610 620 630 640 650
QQSSGLKREV KPEHLAYIIY TSGSTGEPKG VMVEHRSIMN TLNFLESHYP
660 670 680 690 700
VTAEDAYLLK TNYVFDVSIS ELFGWFIGDG RLVILPPNGE KSPQLCMDYI
710 720 730 740 750
ETYKVTHINF VPAMLHVFLE MAKDNKRFTE DGPLKYMMVA GEAFPKVLVK
760 770 780 790 800
KAVSLFTNCR VENIYGPTEA SIYAAYFGCG KGDIASHHTP IGKPVSNTKI
810 820 830 840 850
YIVDQHLKPV PIGKPGELCI AGAGLARGYF KKPGLTAEKF IDNPFESGTK
860 870 880 890 900
LYKSGDSARW LPDGNIEYLG RIDSQVKIRG FRVELGAIET KLGEFPGILD
910 920 930 940 950
QAVVVKQLEG HQQLAAYYTE ESGHASANPK DLRLHLKSSL PEYMIPSHFI
960 970 980 990 1000
RLDELPLSPS GKVNRKELEK REIVFNRRKP NHLQLTEIED QVLRIWEETL
1010 1020 1030 1040 1050
KVSGFGPEDG FFDAGGDSLL AVAVAERIKK EFDCEFHVTE LFEYSTIRAI
1060 1070 1080 1090 1100
SEYILEMKNS DLAGTQNEDD HDDKKDGKYP KQKIPPYFDD SVAIVGISCQ
1110 1120 1130 1140 1150
FPGAKNHHDF WNHIKEGKES IRFFSEEELR ANGVPEELIQ HPDYVPVQSV
1160 1170 1180 1190 1200
IEGKDLFDPG FFQISPKDAE YMDPQLRLLL LHSWKAIEDA GYVAKEIPAT
1210 1220 1230 1240 1250
SVYMSASSNS YRTLLPKETT EGHESPDGYV SWVLAQSGTI PTMISHKLGL
1260 1270 1280 1290 1300
KGPSYFVHSN CSSSLVGLYQ AYKSLTSGES QYALVGGATL HAQSAIGYVH
1310 1320 1330 1340 1350
QNGLNFSSDG HVKAFDASAD GMAGGEGVAV ILLKKAVDAV KDGDHIYAIM
1360 1370 1380 1390 1400
RGIGINNDGA EKAGFYAPSV KGQTEVIQHV LDTTKIHPET VSYIEAHGTG
1410 1420 1430 1440 1450
TKLGDPIEMS ALNKVYKQYT DKTQFCGIGS VKTNIGHLDT AAGLAGCIKV
1460 1470 1480 1490 1500
AMSLYHNELA PTINCTEPNP DIKFESSPFY VVRERKSLEK HAGVHRAALS
1510 1520 1530 1540 1550
SFGLGGTNAH AIFEQYENIS DAGAENEGNQ PYIIPISAKN SERLQVYAKE
1560 1570 1580 1590 1600
MLSYISQDEQ RHFSLRDIAY TFQVGREAMD NRIVFIVNDL EEWKHQLEAF
1610 1620 1630 1640 1650
VTGKPLAEGC IQGEKTRMTS AEQLLGNAEA DDMASSRISK EELRKLAEMW
1660 1670 1680 1690 1700
ANGFHVEWRR LYPNIKPRRI SLPTYPFAEE RYWPESSTGA ITTIEPSRLH
1710 1720 1730 1740 1750
PLVHHNTSVL SEQRFSSIFT GQEYFIAEHI IKGMAILPAA VTLEMARAAI
1760 1770 1780 1790 1800
EQGIGGLEDH ETGIRLKNVV WVRPVVAGSE PVQVNIGLYD EDGGHIAYRM
1810 1820 1830 1840 1850
YGDPESADAE PVVYNQGKAE LIQLKREKAL DLSKIKKQCD QSKMDAASFY
1860 1870 1880 1890 1900
EGMIGADYGP GYKSVEAVYK GDGQLLAKLS LPESVAHTLG DYVLHPSVMD
1910 1920 1930 1940 1950
GALQAAEYLQ NVVRAELSDT EDFKAALPFA LEELEVFRQC VSDMWVYVQF
1960 1970 1980 1990 2000
NSKNKPGDLI QKVDIHLCDE HGMICVRLKG FSTRVMEADI QTEPSKINAE
2010 2020 2030 2040 2050
TLLLQPVWQE QKAANSLAAK KYAEHLVFLC EYDHETRKQI EAAIEDVHVY
2060 2070 2080 2090 2100
SLEARPSSVD GRFHSYTEQV FKKVQEIIRT KPKDGILVQI VTSAEGEQQL
2110 2120 2130 2140 2150
FSGLTGLLKT ACQENAKLTG QMIEVSSEES GESIAGKLLE NQMSSDSYVK
2160 2170 2180 2190 2200
YQNGTRYIAD WREIKQAKGD GSKPWKDNGV YLISGGAGGL GHIFAKEIAE
2210 2220 2230 2240 2250
QTKNATVILA GRSPLSESKS KKLKELHSKG ADITYRQTDV TNKIEVYQLI
2260 2270 2280 2290 2300
DDIQKRYGRL NGILHSAGII KDSYLVNKQA KDLHDVLAPK VKGLVYLDEA
2310 2320 2330 2340 2350
SKDLPLDFFI LFSSLSGSLG SIGQSDYAAA NVFMDMYAGY RNRLADLSQR
2360 2370 2380 2390 2400
HGQTLSVNWP LWRDGGMQVD QETEKRLVQL AGIVPMRAEK GIQALYQALH
2410 2420 2430 2440 2450
SEANQVMVIE GDVQKIKQNM LAKNASAPME KKEAEHMTEQ INSIDADSLL
2460 2470 2480 2490 2500
DKVKAMLKRE IAKLLKVKLE TIDDHAEMTV YGFDSISMTE FTNHINRAYQ
2510 2520 2530 2540 2550
LELTPTVFFD HPTIHAFGKH LSEEYQSVFA KTFAVRAVSA QLQPAAKQEQ
2560 2570 2580 2590 2600
AVRAKAKRRR KQQVMLPNAI QSDAGPEPIA IVGISGIFPM AKDVEAYWNI
2610 2620 2630 2640 2650
LKEGKDCMTE IPKDRWDWRE YEGDPAKEVN KTNVKWGGFI DGIADFDPLF
2660 2670 2680 2690 2700
FGISPREAEQ MEPQQRLLLT YAWKAIEDAG YSAKRLSGTK TGVFIGTGNT
2710 2720 2730 2740 2750
GYSSLLSKAN SAIEGSAAAN TSPSVGPNRV SYFLNLHGPS EPVDTACSSS
2760 2770 2780 2790 2800
LVAIHHAISS IEEGTCDMAL AGGVNTIILP EVYISFDKAG ALSKEGKCKT
2810 2820 2830 2840 2850
FSNQADGFAH GEGAGILFLK KLKAAEEAGD HIYGVIKGSA INHGGRAASL
2860 2870 2880 2890 2900
TTPNPKAQAD VIQSAYQKAG IDPKTVTYIE AHGTGTELGD PVEINGLKSA
2910 2920 2930 2940 2950
FKALGVNEGD TSANPYCGLG SVKTNIGHLS LAAGAAGVIK ILLQLKHKTL
2960 2970 2980 2990 3000
VKSLHCENVN PYIQLKNSPF YIVRETEEWK ALKNEQGEEL PRRAGVSSFG
3010 3020 3030 3040 3050
IGGVNAHVII EEYIPEASDE NIPSIAPEHP GIFVLSAKNE ARLKEHAQQL
3060 3070 3080 3090 3100
ADALDKQTYS DVNLARIAYT LQAGRDAMEE RLGIISGSIE DLQKKLKDFA
3110 3120 3130 3140 3150
AEKSGVEDVF KGRIDKGTLQ MLTEDEEIQE AVEKWMERGK YAKLLELWVK
3160 3170 3180 3190 3200
GLDVDWTKLY GENLPKRISL PTYPFAKDRY WISDHIEKSG SIDANQAASR
3210 3220 3230 3240 3250
LGGAVLHPLM HQNTSNLSEQ RFSSIYTGEE FFLADHVVKG QRILPGVAHL
3260 3270 3280 3290 3300
ELARAAVEQA AEVQGVPRIM KLKNAVWVRP IVVEDQPQQV HIRLLPGENG
3310 3320 3330 3340 3350
EISYEIYGHS DVTGEQSIVY SQGSAVLNPA ENLPAVDLQS LREQCQESHF
3360 3370 3380 3390 3400
SVNEVYDTYR MIGFEYGPAY RGVKKIYTAE QFVLAKLSLH PSAADTLSQY
3410 3420 3430 3440 3450
KMHPGLMDSA LQASSILTGA GDNQLTLPFA VQELEVFGAC SSEMWVYARY
3460 3470 3480 3490 3500
SQGSKATDKV QKRDMDILDE SGNVCVRMKG LSFRAAEGGS GSAESDQTLA
3510 3520 3530 3540 3550
TLMFEEKWVP KDFKKESPEP HYERHIVMLC DMNGLSKDRI ESRMTGAECI
3560 3570 3580 3590 3600
VLESFREGLA ERFQDYAEQA LETVQGLLKS RPQGNVLIQL LTSAQRKQYS
3610 3620 3630 3640 3650
FSGLSALLKT AGLENKKLIG QTIEIDSHEN VESVIEKLKE NKRHTEDQHI
3660 3670 3680 3690 3700
KYEKGKRYIN DLDEMQIDDR EISMPWRDKG VYLITGGAGG LGFIFAKEIA
3710 3720 3730 3740 3750
RQAEQPVLIL TGRSALNADQ QAELNELQQL GARAEYRQVD VTQTEAASEL
3760 3770 3780 3790 3800
ITSITSDYED LNGVIHSAGL IKDNYLMSKT NEELTQVLAP KVKGLVNVDE
3810 3820 3830 3840 3850
ATEHLALDFF ILFSSISSVA GSAGQADYAM ANAFMDSYAA YRNALVTAMY
3860 3870 3880 3890 3900
RHGQTLSINW PLWKEGGMRA NKEIENMTLK NTGVTPMRTE TGIQALYKGL
3910 3920 3930 3940 3950
AFGKDQVIVM EGFKDMMREK LTQKPSSDDV PMKTVQVRVT SEARMDQGNM
3960 3970 3980 3990 4000
FDHIQEVLKQ TISQLLKIKP EEIDPDMEFN QYGFDSITLT EFANTLNEKC
4010 4020 4030 4040 4050
KLDLTPTVFF EHATVYAFAG YLSEEYPNAF TAQTPAKAEV LMQPVEQNIK
4060 4070 4080 4090 4100
NMTFSTENRF VKPSVTPMQK EADHKPEPIA IVGMSGVFPK AKDVEEYWKN
4110 4120 4130 4140 4150
LSSGADCITE VPKDRWDWQE YYGDPLKEAN KTNVKWGGFI DEVADFDPLF
4160 4170 4180 4190 4200
FGISPLEAEQ MEPQQRLLMT YAWKAVEEAG HSARSLAGTK TGIFIGTGNT
4210 4220 4230 4240 4250
GYSSLLSNVD IEGSAAANMS PSAGPNRVSY FLNIHGPSEP IDTACSSSLV
4260 4270 4280 4290 4300
AIHHAVCAIE NGNCEMAIAG GVNTVVTPQG HIAYDKAGAL SKEGRCKTFS
4310 4320 4330 4340 4350
DKADGFAVSE GAGILFLKKL TAAERDGDHI YGVIKGSAVN HGGRANSLTT
4360 4370 4380 4390 4400
PNPKAQADVV KTAYEKAGID PRTVTYIEAH GTGTELGDPV EINGLKAAFK
4410 4420 4430 4440 4450
ELYEKTGDPA VHGSHCGLGS AKTNIGHLSL AAGVAGVIKV LLQLKHKTLV
4460 4470 4480 4490 4500
KSLYSETVNP YIRLDDSPFY IVQESREWQA LRDEAGRELP RRAGISSFGI
4510 4520 4530 4540 4550
GGVNAHVVIE EYIPKETTHP ATAPAVTAQH PGIFILSAKD EDRLKDQARQ
4560 4570 4580 4590 4600
LADFISKRSI TARDLTDIAY TLQEGRDAME ERLGIIAVST GDLLEKLNLF
4610 4620 4630 4640 4650
IEGGTNAKYM YRGRAEKGIA QTLRSDDEVQ KTLNNSWEPH IYERLLDLWV
4660 4670 4680 4690 4700
KGMEIGWSKL YDGKQPKRIS LPTYPFAKER YWITDTKEEA AAHQTALKTV
4710 4720 4730 4740 4750
ESAALHPLIH VNTSDLSEQR FSSAFTGAEF FFADHKVKGK PVMPGVAYLE
4760 4770 4780 4790 4800
MVHAAVTRAV RRTEDQQSVI HIKNVVWVQP IVADGQPVQV DISLNPQQDG
4810 4820 4830 4840 4850
EIAFNVYTEA AHNDRKIHCQ GSASIRGAGD IPVQDISALQ DQCSLSTLSH
4860 4870 4880 4890 4900
DQCYELFKAI GIDYGPGFQG IDRLYIGRNQ ALAELSLPAG VTHTLNEFVL
4910 4920 4930 4940 4950
HPSMADSALQ ASIGLKLNSG DEQLSLPFAL QELEIFSPCT NKMWVSVTSR
4960 4970 4980 4990 5000
PNEDKIQRLD IDLCDEQGRV CVRIKGITSR LLEEGIQPPD GPTSLGNSKA
5010 5020 5030 5040 5050
TLNGALLMAP IWDRVQLEKR SISPADERVV ILGGDDNSRK AVQREFPFAK
5060 5070 5080 5090 5100
ELYIEPNASI HRITGQLEAL GSFDHIVWMS PSRVTECEVG DEMIEAQDQG
5110 5120 5130 5140 5150
VIQMYRLIKA MLSLGYGQKE ISWTIVTVNT QYVDQHDIVD PVDAGVHGLI
5160 5170 5180 5190 5200
GSMSKEYPNW QTKLIDVKKY EDLPLSQLLS LPADQEGNTW AYRNKIWHKL
5210 5220 5230 5240 5250
RLIPVHNNQP VHTKYKHGGV YVVIGGAGGI GEAWSEYMIR TYQAQIVWIG
5260 5270 5280 5290 5300
RRKKDAAIQS KLDRFARLGR APYYIQADAA NREELERAYE TMKQTHREIN
5310 5320 5330 5340 5350
GIIHSAIVLQ DRSLMNMSEE CFRNVLAAKV DVSVRMAQVF RHEPLDFVLF
5360 5370 5380 5390 5400
FSSVQSFARA SGQSNYAAGC SFKDAFAQRL SQVWPCTVAV MNWSYWGSIG
5410 5420 5430 5440 5450
VVSSPDYQKR MAQAGIGSIE APEAMEALEL LLGGPLKQLV MMKMANETND
5460 5470 5480
EAEQTEETIE VYPETHGSAI QKLRSYHPGD NTKIQQLL
Length:5,488
Mass (Da):609,593
Last modified:May 5, 2009 - v3
Checksum:i1EA0D0F91C78FDDD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13604.3.
RefSeqiNP_389602.3. NC_000964.3.
WP_010886514.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13604; CAB13604; BSU17210.
GeneIDi940054.
KEGGibsu:BSU17210.
PATRICi18975251. VBIBacSub10457_1817.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL009126 Genomic DNA. Translation: CAB13604.3.
RefSeqiNP_389602.3. NC_000964.3.
WP_010886514.1. NC_000964.3.

3D structure databases

ProteinModelPortaliO31782.
SMRiO31782. Positions 3-443, 445-973, 979-1057, 1089-1989, 2064-2424, 2454-2523, 2575-3488, 3565-3924, 3954-4024, 4075-4984, 5299-5377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100009466.

Proteomic databases

PaxDbiO31782.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13604; CAB13604; BSU17210.
GeneIDi940054.
KEGGibsu:BSU17210.
PATRICi18975251. VBIBacSub10457_1817.

Phylogenomic databases

eggNOGiENOG4105C0W. Bacteria.
COG1020. LUCA.
HOGENOMiHOG000008929.
InParanoidiO31782.
KOiK13614.
OMAiGPNRVSY.
OrthoDBiEOG6QP0WP.
PhylomeDBiO31782.

Enzyme and pathway databases

UniPathwayiUPA01003.
BioCyciBSUB:BSU17210-MONOMER.

Family and domain databases

Gene3Di1.10.1200.10. 5 hits.
3.10.129.10. 1 hit.
3.40.47.10. 6 hits.
3.40.50.720. 3 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR029069. HotDog_dom.
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. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF16197. KAsynt_C_assoc. 3 hits.
PF00109. ketoacyl-synt. 3 hits.
PF02801. Ketoacyl-synt_C. 3 hits.
PF08659. KR. 3 hits.
PF00550. PP-binding. 3 hits.
PF14765. PS-DH. 3 hits.
[Graphical view]
SMARTiSM00826. PKS_DH. 3 hits.
SM00825. PKS_KS. 3 hits.
SM00823. PKS_PP. 3 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 5 hits.
SSF51735. SSF51735. 4 hits.
SSF53901. SSF53901. 7 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 2 hits.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
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Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. "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 1128-1129 AND 1703.
  3. "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-1018.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  4. Cited for: SUBCELLULAR LOCATION.
    Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
  5. "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 nameiPKSN_BACSU
AccessioniPrimary (citable) accession number: O31782
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 5, 2009
Last modified: July 6, 2016
This is version 117 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 1 domain binds alanine.

Keywords - Technical termi

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. 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.