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P37475

- SP2E_BACSU

UniProt

P37475 - SP2E_BACSU

Protein

Stage II sporulation protein E

Gene

spoIIE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 1 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Normally needed for pro-sigma E processing during sporulation but can be bypassed in vegetative cells. Activates SpoIIAA by dephosphorylation.

    Catalytic activityi

    [a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate.

    Cofactori

    Manganese.

    GO - Molecular functioni

    1. phosphoprotein phosphatase activity Source: UniProtKB-KW

    GO - Biological processi

    1. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Sporulation

    Enzyme and pathway databases

    BioCyciBSUB:BSU00640-MONOMER.

    Protein family/group databases

    PptaseDBiP3D0406130.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Stage II sporulation protein E (EC:3.1.3.16)
    Alternative name(s):
    Stage II sporulation protein H
    Gene namesi
    Name:spoIIE
    Synonyms:spoIIH
    Ordered Locus Names:BSU00640
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU00640. [Micado]

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity
    Note: Polar septum.

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell
    3. prospore membrane Source: CACAO

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 827827Stage II sporulation protein EPRO_0000057794Add
    BLAST

    Proteomic databases

    PaxDbiP37475.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-126037.
    STRINGi224308.BSU00640.

    Structurei

    Secondary structure

    1
    827
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi592 – 6009
    Beta strandi611 – 6177
    Turni618 – 6203
    Beta strandi621 – 6277
    Beta strandi637 – 6404
    Helixi642 – 65312
    Helixi657 – 66812
    Beta strandi673 – 6753
    Beta strandi680 – 6867
    Turni687 – 6893
    Beta strandi691 – 6988
    Beta strandi702 – 7065
    Beta strandi709 – 7124
    Beta strandi728 – 7347
    Beta strandi740 – 7445
    Helixi746 – 7494
    Beta strandi752 – 7543
    Helixi758 – 76710
    Helixi774 – 78815
    Beta strandi797 – 80610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3T91X-ray2.64A/B590-827[»]
    3T9QX-ray2.76A/B590-827[»]
    ProteinModelPortaliP37475.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini341 – 827487CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei49 – 6921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei71 – 9121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei116 – 13621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei142 – 16221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei175 – 19521HelicalSequence AnalysisAdd
    BLAST
    Transmembranei206 – 22621HelicalSequence AnalysisAdd
    BLAST
    Transmembranei247 – 26721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei269 – 28921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei299 – 31921HelicalSequence AnalysisAdd
    BLAST
    Transmembranei320 – 34021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini605 – 827223PP2C-likeAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi799 – 8024Poly-Val

    Sequence similaritiesi

    Contains 1 PP2C-like domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG2208.
    HOGENOMiHOG000082091.
    KOiK06382.
    OMAiDGMGNGE.
    OrthoDBiEOG6JMMQ9.
    PhylomeDBiP37475.

    Family and domain databases

    Gene3Di3.60.40.10. 1 hit.
    InterProiIPR001932. PP2C-like_dom.
    IPR014221. Spore_II_E.
    [Graphical view]
    PfamiPF07228. SpoIIE. 1 hit.
    [Graphical view]
    SMARTiSM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view]
    SUPFAMiSSF81606. SSF81606. 1 hit.
    TIGRFAMsiTIGR02865. spore_II_E. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P37475-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEKAERRVNG PMAGQALEKL QSFFNRGTKL VTHHLHSLFF YKGFIYVVIG    50
    FLLGRAFILS EVLPFALPFF GAMLLIRRDK AFYAVLAVLA GALTISPKHS 100
    LLILAALLAF FVFSKVAAFI TDDRVKALPI VVFFSMAAAR AGFVYAQNGV 150
    FTTYDYVMAI VEAGLSFILT LIFLQSLPIF TVKKVKQSLK IEEIICFMIL 200
    IASVLTGLAG LSYQGMQAEH ILARYVVLSF SFIGGASIGC TVGVVTGLIL 250
    GLANIGNLYQ MSLLAFSGLL GGLLKEGKKA GAAIGLIVGS LLISLYGEGS 300
    AGLMTTLYES LIAVCLFLLT PQSITRKVAR YIPGTVEHLQ EQQQYARKIR 350
    DVTAQKVDQF SNVFHALSES FATFYQASDE QTDDSEVDLF LSKITEHSCQ 400
    TCYKKNRCWV QNFDKTYDLM KQVMLETEEK EYASNRRLKK EFQQYCSKSK 450
    QVEELIEDEL AHHHAHLTLK KKVQDSRRLV AEQLLGVSEV MADFSREIKR 500
    EREQHFLQEE QIIEALQHFG IEIQHVEIYS LEQGNIDIEM TIPFSGHGES 550
    EKIIAPMLSD ILEEQILVKA EQHSPHPNGY SHVAFGSTKS YRVSTGAAHA 600
    AKGGGLVSGD SYSMMELGAR KYAAAISDGM GNGARAHFES NETIKLLEKI 650
    LESGIDEKIA IKTINSILSL RTTDEIYSTL DLSIIDLQDA SCKFLKVGST 700
    PSFIKRGDQV MKVQASNLPI GIINEFDVEV VSEQLKAGDL LIMMSDGIFE 750
    GPKHVENHDL WMKRKMKGLK TNDPQEIADL LMEEVIRTRS GQIEDDMTVV 800
    VVRIDHNTPK WASIPVPAIF QNKQEIS 827
    Length:827
    Mass (Da):91,969
    Last modified:October 1, 1994 - v1
    Checksum:i33EA3A81935B407B
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26185 Genomic DNA. Translation: BAA05299.1.
    U26835 Genomic DNA. Translation: AAB58073.1.
    AL009126 Genomic DNA. Translation: CAB11840.1.
    M29403 Genomic DNA. Translation: AAA22798.1.
    L23497 Genomic DNA. Translation: AAB38381.1.
    PIRiS66094.
    RefSeqiNP_387945.1. NC_000964.3.
    WP_003243026.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB11840; CAB11840; BSU00640.
    GeneIDi938480.
    KEGGibsu:BSU00640.
    PATRICi18971603. VBIBacSub10457_0065.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D26185 Genomic DNA. Translation: BAA05299.1 .
    U26835 Genomic DNA. Translation: AAB58073.1 .
    AL009126 Genomic DNA. Translation: CAB11840.1 .
    M29403 Genomic DNA. Translation: AAA22798.1 .
    L23497 Genomic DNA. Translation: AAB38381.1 .
    PIRi S66094.
    RefSeqi NP_387945.1. NC_000964.3.
    WP_003243026.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3T91 X-ray 2.64 A/B 590-827 [» ]
    3T9Q X-ray 2.76 A/B 590-827 [» ]
    ProteinModelPortali P37475.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-126037.
    STRINGi 224308.BSU00640.

    Protein family/group databases

    PptaseDBi P3D0406130.

    Proteomic databases

    PaxDbi P37475.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB11840 ; CAB11840 ; BSU00640 .
    GeneIDi 938480.
    KEGGi bsu:BSU00640.
    PATRICi 18971603. VBIBacSub10457_0065.

    Organism-specific databases

    GenoListi BSU00640. [Micado ]

    Phylogenomic databases

    eggNOGi COG2208.
    HOGENOMi HOG000082091.
    KOi K06382.
    OMAi DGMGNGE.
    OrthoDBi EOG6JMMQ9.
    PhylomeDBi P37475.

    Enzyme and pathway databases

    BioCyci BSUB:BSU00640-MONOMER.

    Family and domain databases

    Gene3Di 3.60.40.10. 1 hit.
    InterProi IPR001932. PP2C-like_dom.
    IPR014221. Spore_II_E.
    [Graphical view ]
    Pfami PF07228. SpoIIE. 1 hit.
    [Graphical view ]
    SMARTi SM00331. PP2C_SIG. 1 hit.
    SM00332. PP2Cc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF81606. SSF81606. 1 hit.
    TIGRFAMsi TIGR02865. spore_II_E. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
      Ogasawara N., Nakai S., Yoshikawa H.
      DNA Res. 1:1-14(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "Structure and function of the Bacillus SpoIIE protein and its localization to sites of sporulation septum assembly."
      Barak I., Behari J., Olmedo G., Guzman P., Brown D.P., Castro E., Walker D., Westpheling J., Youngman P.
      Mol. Microbiol. 19:1047-1060(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168 / PY79.
    3. "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.
    4. "Characterization of the promoter region of the Bacillus subtilis spoIIE operon."
      Guzman P., Westpheling J., Youngman P.
      J. Bacteriol. 170:1598-1609(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
    5. "Characterization of a cell division gene from Bacillus subtilis that is required for vegetative and sporulation septum formation."
      Levin P.A., Losick R.
      J. Bacteriol. 176:1451-1459(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
      Strain: 168.
    6. "Activation of cell-specific transcription by a serine phosphatase at the site of asymmetric division."
      Duncan L., Alper S., Arigoni F., Losick R., Stragier P.
      Science 270:641-644(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.

    Entry informationi

    Entry nameiSP2E_BACSU
    AccessioniPrimary (citable) accession number: P37475
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 117 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3