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Protein

Plipastatin synthase subunit E

Gene

ppsE

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 acid Ile as part of the biosynthesis of the lipopeptide antibiotic plipastatin. The activation sites for this amino acid consist of individual domains.1 Publication

Cofactori

pantetheine 4'-phosphateCuratedNote: Binds 1 phosphopantetheine 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:BSU18300-MONOMER.

Protein family/group databases

ESTHERibacsu-PPSE. Thioesterase.

Names & Taxonomyi

Protein namesi
Recommended name:
Plipastatin synthase subunit E (EC:2.3.1.-)
Alternative name(s):
Peptide synthase 5
Including the following 1 domains:
ATP-dependent isoleucine adenylase
Short name:
IsoA
Alternative name(s):
Isoleucine activase
Gene namesi
Name:ppsE
Synonyms:pps5
Ordered Locus Names:BSU18300
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12791279Plipastatin synthase subunit EPRO_0000360845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1010 – 10101O-(pantetheine 4'-phosphoryl)serinePROSITE-ProRule annotation

Keywords - PTMi

Phosphopantetheine, Phosphoprotein

Proteomic databases

PaxDbiO31827.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010086.

Structurei

3D structure databases

ProteinModelPortaliO31827.
SMRiO31827. Positions 12-453, 456-964, 971-1269.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini980 – 104768Acyl carrierPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni14 – 10471034Domain (isoleucine-activating)Add
BLAST
Regioni14 – 317304CondensationAdd
BLAST
Regioni503 – 898396AdenylationAdd
BLAST
Regioni1068 – 1273206ThioesteraseAdd
BLAST

Sequence similaritiesi

Contains 1 acyl carrier domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG3319. LUCA.
HOGENOMiHOG000229993.
InParanoidiO31827.
KOiK15668.
OMAiPISGFGI.
OrthoDBiEOG6HJ25P.
PhylomeDBiO31827.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR025110. AMP-bd_C.
IPR020459. AMP-binding.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
PRINTSiPR00154. AMPBINDING.
SMARTiSM00823. PKS_PP. 1 hit.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O31827-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKGADTMNT IKKIKNIYPL SHMQEGMLFH SFLRKEEGAY VEQSLFTIKG
60 70 80 90 100
SLSYDWFQRS IQAIIDRHDI FRTVFLPHVP HLSGPRQVVM TEREFHLNSE
110 120 130 140 150
DISHLPTNDQ NEYIERFKEK DKQKGFDLQK DMLMRISLFK TAKDEHVCIW
160 170 180 190 200
SHHHILMDGW CLGIVMQEFM QIYQSIHAGK PLSLDPVRPY STYISWLTNR
210 220 230 240 250
DKEKAAAYWD TYLKNYSAPS PLPRVSDKET KESYHREDLI FSLNKPLTDK
260 270 280 290 300
LKETAKQHGV TLATLIQAVW GVMLQQYNRT DDVVFGAVVS GRPSEIPGVE
310 320 330 340 350
QMIGLFINTI PIRIKTHQDE TFHELLIRCQ KEMLEAEPFT CQPLFDIQAN
360 370 380 390 400
TALKQELIDH IIVFENYPLQ QKIADSADQT DSPLQIDQVQ VSEQSGYNFN
410 420 430 440 450
LVVAPGEELV IKFSYNAFVY DAAWISCIKR QFTQALSTAA QHPHMPIADF
460 470 480 490 500
SFLDATEKEQ IVTQFNNTKT EYPKNHTIID LFREQAEKTP DHTALVYGNM
510 520 530 540 550
SISYKELDKR SNALARELIQ KGFRKNETAG ILAAHSPEFM ISVLAVLKAG
560 570 580 590 600
GAYLPLDAEL PPERVSFMLE ETQAKMLIVQ KGLEQNAAFS GTCIISDAQG
610 620 630 640 650
LMEENDIPIN ISSSPDDLAY IMYTSGSTGR PKGVMITNRN VVSLVRNSNY
660 670 680 690 700
TSASGDDRFI MTGSISFDAV TFEMFGALLN GASLHIIDKS TMLTPDRFGA
710 720 730 740 750
YLLENDITVL FLTTALFNQL AQVRADMFRG LHTLYVGGEA LSPALMNAVR
760 770 780 790 800
HACPDLALHN IYGPTENTTF STFFEMKRDY AGPIPIGKPI SNSTAYILDT
810 820 830 840 850
KGRLLPIGVP GELCVGGDGV AKGYLNRVDL TNAVFSPHPF LPGERIYRTG
860 870 880 890 900
DLARWLPDGN LEYISRIDRQ MKIRGKRIEP AEIEARLLEM EGVQEAAVTL
910 920 930 940 950
REKDGEAQLY THYVGDHKKT DTDFRADLAR VLPDYMIPQH WVRVERMPLT
960 970 980 990 1000
GNGKIDRSAL PIPENKPAKR QNIILPRNLV EEELANIWKQ VLGVNTISID
1010 1020 1030 1040 1050
DDFFAIGGHS LRALQVIHTL KHQQNIDIPI DFLFEHPTIA QLAEKLYSKQ
1060 1070 1080 1090 1100
LTAANEQHVI KLNQHGAQNL FCFPPISGFG IYFKDLALLL NEKAAVYGFH
1110 1120 1130 1140 1150
FIEQDTRIEQ YVNCMTDIQP EGPYVLLGYS AGGNLAFEVA QAMERKGLEV
1160 1170 1180 1190 1200
SDFIIVDAYL KEQPLPIDTG NDESAAYLPE AVREKVMKKK RNYQEYWAQL
1210 1220 1230 1240 1250
LNEGHIKASI HFIEAGIHPE TSGHTGLTKW EGACGNYSEY TGFGAHKDML
1260 1270
EGTYAEKNAD IILDILEKIT SNQVILHKR
Length:1,279
Mass (Da):144,619
Last modified:January 1, 1998 - v1
Checksum:i22EA638DEF0CEBE0
GO

Sequence cautioni

The sequence CAA74213.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13917 Genomic DNA. Translation: CAA74213.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB13713.1.
PIRiE69681.
RefSeqiNP_389712.1. NC_000964.3.
WP_010886522.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13713; CAB13713; BSU18300.
GeneIDi939956.
KEGGibsu:BSU18300.
PATRICi18975497. VBIBacSub10457_1940.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y13917 Genomic DNA. Translation: CAA74213.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB13713.1.
PIRiE69681.
RefSeqiNP_389712.1. NC_000964.3.
WP_010886522.1. NC_000964.3.

3D structure databases

ProteinModelPortaliO31827.
SMRiO31827. Positions 12-453, 456-964, 971-1269.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100010086.

Protein family/group databases

ESTHERibacsu-PPSE. Thioesterase.

Proteomic databases

PaxDbiO31827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB13713; CAB13713; BSU18300.
GeneIDi939956.
KEGGibsu:BSU18300.
PATRICi18975497. VBIBacSub10457_1940.

Phylogenomic databases

eggNOGiCOG3319. LUCA.
HOGENOMiHOG000229993.
InParanoidiO31827.
KOiK15668.
OMAiPISGFGI.
OrthoDBiEOG6HJ25P.
PhylomeDBiO31827.

Enzyme and pathway databases

BioCyciBSUB:BSU18300-MONOMER.

Family and domain databases

Gene3Di1.10.1200.10. 1 hit.
3.40.50.1820. 2 hits.
InterProiIPR010071. AA_adenyl_domain.
IPR029058. AB_hydrolase.
IPR025110. AMP-bd_C.
IPR020459. AMP-binding.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR020806. PKS_PP-bd.
IPR020802. PKS_thioesterase.
IPR009081. PP-bd_ACP.
IPR006162. Ppantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]
PfamiPF00501. AMP-binding. 1 hit.
PF13193. AMP-binding_C. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]
PRINTSiPR00154. AMPBINDING.
SMARTiSM00823. PKS_PP. 1 hit.
SM00824. PKS_TE. 1 hit.
[Graphical view]
SUPFAMiSSF47336. SSF47336. 1 hit.
SSF53474. SSF53474. 1 hit.
TIGRFAMsiTIGR01733. AA-adenyl-dom. 1 hit.
PROSITEiPS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence completion, identification and definition of the fengycin operon in Bacillus subtilis 168."
    Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V.
    Microbiology 143:3443-3450(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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. "The genes degQ, pps, and lpa-8 (sfp) are responsible for conversion of Bacillus subtilis 168 to plipastatin production."
    Tsuge K., Ano T., Hirai M., Nakamura Y., Shoda M.
    Antimicrob. Agents Chemother. 43:2183-2192(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PLIPASTATIN BIOSYNTHESIS.

Entry informationi

Entry nameiPPSE_BACSU
AccessioniPrimary (citable) accession number: O31827
Secondary accession number(s): Q799M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 20, 2009
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 104 of the entry and version 1 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.