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Protein

Plipastatin synthase subunit D

Gene

ppsD

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

Functioni

This protein is a multifunctional enzyme, able to activate and polymerize the amino acids Pro, Gln and Tyr as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue is further epimerized to the D-isomer form. The activation sites for these amino acids consist of individual domains.1 Publication

Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 3 phosphopantetheines covalently.Curated

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU18310-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Plipastatin synthase subunit D (EC:2.3.1.-)
Alternative name(s):
Peptide synthase 4
Including the following 3 domains:
ATP-dependent proline adenylase
Short name:
ProA 1
Alternative name(s):
Proline activase 1
ATP-dependent glutamine adenylase
Short name:
GlnA
Alternative name(s):
Glutamine activase
ATP-dependent tyrosine adenylase 2
Short name:
TyrA 2
Alternative name(s):
Tyrosine activase 2
Gene namesi
Name:ppsD
Synonyms:pps4
Ordered Locus Names:BSU18310
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 36033603Plipastatin synthase subunit DPRO_0000360844Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1001 – 10011O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei2032 – 20321O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation
Modified residuei3069 – 30691O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiP94459.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010091.

Structurei

3D structure databases

ProteinModelPortaliP94459.
SMRiP94459. Positions 4-443, 460-956, 962-1470, 1495-1985, 1993-2510, 2513-3024, 3029-3107.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini971 – 103868Acyl carrier 1PROSITE-ProRule annotationAdd
BLAST
Domaini2002 – 206968Acyl carrier 2PROSITE-ProRule annotationAdd
BLAST
Domaini3039 – 310567Acyl carrier 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 10431037Domain 1 (proline-activating)Add
BLAST
Regioni7 – 306300Condensation 1Add
BLAST
Regioni490 – 889400Adenylation 1Add
BLAST
Regioni1053 – 20691017Domain 2 (glutamine-activating)Add
BLAST
Regioni1053 – 1334282Condensation 2Add
BLAST
Regioni1521 – 1924404Adenylation 2Add
BLAST
Regioni2084 – 35961513Domain 3 (proline-activating)Add
BLAST
Regioni2084 – 2374291Condensation 3Add
BLAST
Regioni2560 – 2956397Adenylation 3Add
BLAST
Regioni3116 – 3596481EpimerizationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2178 – 21814Poly-Ala

Sequence similaritiesi

Contains 3 acyl carrier domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000229991.
InParanoidiP94459.
KOiK15667.
OMAiARITINY.
PhylomeDBiP94459.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00501. AMP-binding. 3 hits.
PF13193. AMP-binding_C. 3 hits.
PF00668. Condensation. 4 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 2 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 3 hits.
TIGR01720. NRPS-para261. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 3 hits.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P94459-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKANSIQDI YPLSYMQEGM LFHSLLQKDS QAYVEQASFT IEGKVNPQFF
60 70 80 90 100
QNSINALVER HDIFRTIFIS QNVSSPQQVV LRERNVIVLE EDITHLNEAE
110 120 130 140 150
QSQFIEQWKE KDRDRGFHLQ KDVLMRIALI QTGESQYSCI WTFHHIMMDG
160 170 180 190 200
WCLSIVLKEF LHIYASYVNA SPITLEPVQP YGKYIKWLME QDKEQAVSYW
210 220 230 240 250
DHYLSGHEQQ TVLPKQKKTK GKSRQEHVTF SFSKEESSRL SELAAREEVT
260 270 280 290 300
LSTIFHTIWG ILLQKYNNND DAVFGSVISG RPAEIEGIEH MVGLFINTMP
310 320 330 340 350
VRVQGAKTPF LQLIKDMQKD RLAAEAYSYH PLYEIQSRSA VKQGLIDHIL
360 370 380 390 400
VFENYPVQQE IQMLNKQEHA SDLFQIHNFT VADETNYSFY LMVAPGEEIH
410 420 430 440 450
IKMNYDAEQH DRSFVLSVKE HLLNAVSQIL NNPNLPPEEI DITTDTEKRQ
460 470 480 490 500
LIGEITDQTP VYETIHAMFE KQAEKTPDAH AVIDQACSLT YRELNKAANR
510 520 530 540 550
LARHLRMKGV VRQEPVAIMM ERSAAFITGV LGILKAGGAI VPVDPHYPAD
560 570 580 590 600
RIRYILHDCG CSHVVSQAHL PSSLEDNYII THPEDIESKV DGSNIKSVNN
610 620 630 640 650
ADDLLYMIYT SGTTGKPKGV QFEHRNMANL LKFEYTHSGI DFEADVLQFA
660 670 680 690 700
TPSFDVCYQE IFSALLKGGT LHIVPEAIKR DVPQLFAFIN KHQTNIVFLP
710 720 730 740 750
TAFIKMIFSE RELANSFPDG VKHLIAAGEQ LMISDLFQDV LRKRGIHLHN
760 770 780 790 800
HYGPSETHVV STYTIHPGDP IPELPPIGKP IGCTDLYILN HQKQLQPCGV
810 820 830 840 850
PGELYISGAS VARGYVNHDK LTSDKFSSDP FKPDVIMYRT GDLARRLEDG
860 870 880 890 900
NIEYIGRADN QVKIRGYRIE PQEIEVTLMN HPDISEAAIL IWQDQNGEHE
910 920 930 940 950
LCAYYCSVQK LNTIDLRSYM ASELPEYMIP AKWIWVDSIP LTPNGKVDRA
960 970 980 990 1000
ALPEPDASIS GNPYTAPRNL LEAKLSQLFE DVLKNGHIGI QDNFFDNGGH
1010 1020 1030 1040 1050
SLKATVLMSR IAKEFHVQVS LKDIFAHPTV EGLALIIREA EQNLYAAIEP
1060 1070 1080 1090 1100
AEKRDTYPVS SAQKRIYVLQ QLDEGVAYNM PAVLELEGAL DVAKLSAVCK
1110 1120 1130 1140 1150
ELISRHEPLR TSFVSGADDE PVQRIHTEVP FTLSKETTIE GFVRPFDLSQ
1160 1170 1180 1190 1200
APLFRAGLIE VSNEKHVLLV DMHHIISDGV SVQLLIREFT DLYANRQLKP
1210 1220 1230 1240 1250
LRIQYKDYAV WQQKFKKGDS YQKQETYWQQ QFSGDLPILE LPTDKRRPAE
1260 1270 1280 1290 1300
RQFIGGKVTF QLDKEITARI KRLAHKNRST LYMTLLALYS AFLSRLSGQD
1310 1320 1330 1340 1350
DIVIGSPIAG RPHADLEAVL GMFVNTLALR TRPAGNKTFE EFLKEVRQTA
1360 1370 1380 1390 1400
LEAYEHQDYP FEELVDKLGV QREMSRNPLF DTTLVLQNME QQKLKMNDVQ
1410 1420 1430 1440 1450
LQWNDLEHPI SKFDISLYVT EHDSELFCQF EYSTALFEKE TIQRWASLFT
1460 1470 1480 1490 1500
TLVEHTAASP ETELDNIPIL TKEEERDFIE SCHLFEETGY SMNQTLHYAL
1510 1520 1530 1540 1550
EQQAEKTPDQ AAVIFEDGVM TYKELNEQAN RIAWELIGRG VKPETTVAII
1560 1570 1580 1590 1600
GKRSPEMLLG IYGILKAGGA YLPIDPDYPE ERISFLLEDS GTNILLLQSA
1610 1620 1630 1640 1650
GLHVPEFTGE IVYLNQTNSG LAHRLSNPNV DVLPQSLAYV IYTSGSTGMP
1660 1670 1680 1690 1700
KGVEIEHRSA VNFLNSLQSR YQLKHSDMIM HKTSYSFDAS IWELFWWPYA
1710 1720 1730 1740 1750
GASVYLLPQG GEKEPEVIAK AIEEQKITAM HFVPSMLHAF LEHIKYRSVP
1760 1770 1780 1790 1800
IKTNRLKRVF SGGEQLGTHL VSRFYELLPN VSITNSYGPT EATVEAAFFD
1810 1820 1830 1840 1850
CPPHEKLERI PIGKPVHHVR LYLLNQNQRM LPVGCIGELY IAGAGVARGY
1860 1870 1880 1890 1900
LNRPALTEER FLEDPFYPGE RMYKTGDVAR WLPDGNVEFL GRTDDQVKIR
1910 1920 1930 1940 1950
GYRIEPGEIE AALRSIEGVR EAAVTVRTDS GEPELCAYVE GLQRNEVRAQ
1960 1970 1980 1990 2000
LERLLPGYMV PAYMIEMEQW PVTPSGKLDR NALPAPGGAA DAETYTAPRN
2010 2020 2030 2040 2050
VTEMKLSQLW EDVLKNGPVG IHDNFFDRGG HSLKATALVS RITKEFDVQV
2060 2070 2080 2090 2100
PLKDVFAHPT VEGLATVIRE GTDSPYEAIK PAEKQETYPV SSAQKRIYVL
2110 2120 2130 2140 2150
QQLEDGGTGY NMPAVLELEG KLNPERMDRA FQELIKRHES LRTSFEQDEG
2160 2170 2180 2190 2200
GDPVQRIHDE VPFTLQTTVL GARTEQEAAA AFIKPFDLSQ APLFRAQIVK
2210 2220 2230 2240 2250
VSDERHLLLV DMHHIISDGV SVNILIQEFG ELYNNRKLPA LRIQYKDYAV
2260 2270 2280 2290 2300
WQEGFKTGDA YKMQEAYWLK QLEGELPVLD LPADHARPPV RSFAGDKVSF
2310 2320 2330 2340 2350
TLEPEVASGL HKLARENGST LYMVLLAAYT AFLSRLSGQE DIIVGSPIAG
2360 2370 2380 2390 2400
RPHKDLEPIL GMFVNTLALR TRPEGGKPFV QYLQEVRETA LEAFEHQNYP
2410 2420 2430 2440 2450
FEELVDKLEL TRDMSRNPVF DAMLVVQNND YEPLHLHDLQ MKPAQVSHLV
2460 2470 2480 2490 2500
SKFDLTLQAS EGDGNIHFLF EYSTALFEKT TIERWASHLT NVLSIIGKNP
2510 2520 2530 2540 2550
KVTLNHIDIL TQEERHQLLN EFNTGQANQY GVQTISQLFE QQAARTPKAS
2560 2570 2580 2590 2600
ALVSGDKTLT YQELDEWSNG IARALRSRGV KPDTPVGIMM HRSFSMIASI
2610 2620 2630 2640 2650
LGVWKAGGCY VPIDPEYPKE RKRYILSDSG TKLLMTINEA DLGVLADFEG
2660 2670 2680 2690 2700
EILTIESVEE DDKSPLPQMS SAHHLAYIIY TSGTTGRPKG VMVEHKGIAN
2710 2720 2730 2740 2750
TLQWRRNAYA FNETDTILQL FSFSFDGFIT SMFTPLLSGA KAVLLHEEEA
2760 2770 2780 2790 2800
KDILAIKHQL SRQRITHMII VPVLYRALLD VVQPEDVKTL RVVTLAGEAA
2810 2820 2830 2840 2850
DRELIARSLA ICPHTELANE YGPTENSVAT TVMRHMEKQA YVSIGQPIDG
2860 2870 2880 2890 2900
TQVLILNSNH QLQPIGVAGE LCIAGTGLAR GYVNLPELTE RAFTQNPFKP
2910 2920 2930 2940 2950
EARMYRTGDA ARWMADGTLE YLGRIDDQVK IRGYRVETKE IESVIRCIKG
2960 2970 2980 2990 3000
VKDAAVVAHV TASGQTELSA YVVTKPGLST NAVRSELQNK LPVFMHPAFI
3010 3020 3030 3040 3050
EKLDSLPLSP NGKLDRGALP KPVYNHEGER PFLPPSSKME QILADIWKEV
3060 3070 3080 3090 3100
LGAEKIGTAD SFFELGGDSI KALQVSARLH RIGKQMAVKD LFSHPTIQEL
3110 3120 3130 3140 3150
AAYIRDSDTS SSQAAVEGDV QWSPVQKWFL SQDIKEKHHF NQSVMLHRST
3160 3170 3180 3190 3200
SVQEDALRKT LKAITCHHDA LRMVFTQNEQ GKWDQYNRPL SHSDDALYGL
3210 3220 3230 3240 3250
QMIDLSAPDG TDGNRPYEPL IKRHVLDIQQ KMDLKNGPLL QAGLFHTIDG
3260 3270 3280 3290 3300
DFLFLSAHHL VVDGISWRVL LEDLALGYRQ AAGGEDIKLP PKTSSFKAYA
3310 3320 3330 3340 3350
KKLSDYAESQ QLMKQLKYWR EAEEYQTEAL PFDQIDGTRA HEGQRSTISF
3360 3370 3380 3390 3400
TLNDKETAAL LKDANSAYNT DTQDMLLASV ILALRHWTNQ SAFKLSLEGH
3410 3420 3430 3440 3450
GREDVLKGID VSRTIGWFTA IYPLLIKLNA DLPDSEESMV HVLKTTKDTL
3460 3470 3480 3490 3500
RRVPDKGFGY GVIKYLTPPG KKDINFTGAP EISFNYLGQF ESGRTAEVPE
3510 3520 3530 3540 3550
EDAFSFSPLG AGGDISTTWN REQSLDISAI AAEGKLTVNM TYDNARFQRK
3560 3570 3580 3590 3600
TIEQLSETCR QFLLQLIEHC QNKSETEKTI SDFDDQELTE DALQEIADML

SFH
Length:3,603
Mass (Da):406,812
Last modified:June 16, 2009 - v2
Checksum:i9A30389D45FEC274
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti46 – 461N → T in CAA84363 (PubMed:7711903).Curated
Sequence conflicti1293 – 12931L → W in CAA84363 (PubMed:7711903).Curated
Sequence conflicti1303 – 13031V → A in CAA84363 (PubMed:7711903).Curated
Sequence conflicti1324 – 13241V → A in CAA84363 (PubMed:7711903).Curated
Sequence conflicti1530 – 15301N → T in CAA84363 (PubMed:7711903).Curated
Sequence conflicti1533 – 15331A → S in CAA84363 (PubMed:7711903).Curated
Sequence conflicti1743 – 17431H → Q in CAA84363 (PubMed:7711903).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z34883 Genomic DNA. Translation: CAA84363.1.
AL009126 Genomic DNA. Translation: CAB13714.2.
PIRiD69681.
RefSeqiNP_389713.2. NC_000964.3.
WP_009967354.1. NZ_CP010052.1.

Genome annotation databases

EnsemblBacteriaiCAB13714; CAB13714; BSU18310.
GeneIDi940013.
KEGGibsu:BSU18310.
PATRICi18975499. VBIBacSub10457_1941.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z34883 Genomic DNA. Translation: CAA84363.1.
AL009126 Genomic DNA. Translation: CAB13714.2.
PIRiD69681.
RefSeqiNP_389713.2. NC_000964.3.
WP_009967354.1. NZ_CP010052.1.

3D structure databases

ProteinModelPortaliP94459.
SMRiP94459. Positions 4-443, 460-956, 962-1470, 1495-1985, 1993-2510, 2513-3024, 3029-3107.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010091.

Proteomic databases

PaxDbiP94459.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13714; CAB13714; BSU18310.
GeneIDi940013.
KEGGibsu:BSU18310.
PATRICi18975499. VBIBacSub10457_1941.

Phylogenomic databases

eggNOGiENOG4105CEY. Bacteria.
COG0318. LUCA.
HOGENOMiHOG000229991.
InParanoidiP94459.
KOiK15667.
OMAiARITINY.
PhylomeDBiP94459.

Enzyme and pathway databases

BioCyciBSUB:BSU18310-MONOMER.

Family and domain databases

Gene3Di1.10.1200.10. 3 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR025110. AMP-bd_C.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR010060. NRPS_synth.
IPR020806. PKS_PP-bd.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
[Graphical view]
PfamiPF00501. AMP-binding. 3 hits.
PF13193. AMP-binding_C. 3 hits.
PF00668. Condensation. 4 hits.
PF00550. PP-binding. 3 hits.
[Graphical view]
SMARTiSM00823. PKS_PP. 2 hits.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 3 hits.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 3 hits.
TIGR01720. NRPS-para261. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 3 hits.
PS00455. AMP_BINDING. 3 hits.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPPSD_BACSU
AccessioniPrimary (citable) accession number: P94459
Secondary accession number(s): Q796G3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: June 16, 2009
Last modified: September 7, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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. 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.