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P21458

- SP3E_BACSU

UniProt

P21458 - SP3E_BACSU

Protein

DNA translocase SpoIIIE

Gene

spoIIIE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (26 May 2009)
      Previous versions | rss
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    Functioni

    Plays an essential role during sporulation. Required for the translocation of the chromosomal DNA from mother cell into the forespore during polar septation, for the final steps of compartmentalization in the presence of trapped DNA, and for the final steps of engulfment. The N-terminus mediates localization to the division septum and is required for both septal membrane fusion and engulfment membrane fusion. May form DNA-conducting channels across the two lipid bilayers of the septum after cell division. The C-terminus functions as a DNA motor that exports DNA in an ATP-dependent manner from mother cell into the forespore. DNA-binding proteins are stripped off the chromosome during translocation, which may play a key role in reprogramming developmental gene expression in the forespore. The two arms of the chromosome are simultaneously pumped into the forespore, which suggests that the septum contains at least two channels, one for each arm. Required for separation of chromosome termini. Also required for optimal chromosome partitioning in vegetative cells, by actively moving chromosomal DNA trapped within the division septum into the daughter cells.13 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi470 – 4756ATPCurated

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. nucleoside-triphosphatase activity Source: InterPro

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cell division Source: UniProtKB-KW
    3. chromosome segregation Source: UniProtKB-KW
    4. sporulation resulting in formation of a cellular spore Source: UniProtKB-KW

    Keywords - Biological processi

    Cell cycle, Cell division, Chromosome partition, Sporulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU16800-MONOMER.

    Protein family/group databases

    TCDBi3.A.12.1.1. the septal dna translocator (s-dna-t) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA translocase SpoIIIE
    Alternative name(s):
    Stage III sporulation protein E
    Gene namesi
    Name:spoIIIE
    Synonyms:ftsK
    Ordered Locus Names:BSU16800
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU16800. [Micado]

    Subcellular locationi

    Cell membrane 5 Publications; Multi-pass membrane protein 5 Publications
    Note: Localizes to the middle of the sporulation septum, then moves to the forespore pole before the completion of engulfment. Delocalizes after membrane fusion is complete. During sporulation, is exclusively assembled on the mother-cell side of the septum. During vegetative growth, assembles at the division septum when DNA is entrapped in the membranes.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Cells lacking this gene show a chromosome translocation defect and aberrant compartmentalization of both sigma-F and sigma-E, and fail to complete membrane fusion at the end of engulfment.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi467 – 4671G → S in SpoIIIE-73-11; defects in DNA translocation. Can complete engulfment and membrane fusion.
    Mutagenesisi473 – 4731K → A: Abolishes ATP-binding and DNA translocation. 1 Publication
    Mutagenesisi584 – 5841D → A: Decrease in DNA transport. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 787787DNA translocase SpoIIIEPRO_0000098239Add
    BLAST

    Proteomic databases

    PaxDbiP21458.

    Interactioni

    Subunit structurei

    Homohexamer. Forms a ring that surrounds DNA. Assembles into complexes that could contain two hexamers.1 Publication

    Protein-protein interaction databases

    IntActiP21458. 1 interaction.
    STRINGi224308.BSU16800.

    Structurei

    3D structure databases

    ProteinModelPortaliP21458.
    SMRiP21458. Positions 316-706, 714-781.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini175 – 787613CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei22 – 4221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei51 – 7121HelicalSequence AnalysisAdd
    BLAST
    Transmembranei87 – 10721HelicalSequence AnalysisAdd
    BLAST
    Transmembranei154 – 17421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini450 – 646197FtsKPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    Consists of an N-terminal domain, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. Specific interactions between the gamma subdomain and specific SpoIIIE recognition sequences (SRS) regulate the compartment-specific activation of a mother-cell SpoIIIE complex. Interactions with nonpermissive SRS in the forespore lead to inactivation of the complex.2 Publications

    Sequence similaritiesi

    Belongs to the FtsK/SpoIIIE/SftA family.Curated
    Contains 1 FtsK domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1674.
    HOGENOMiHOG000010003.
    OrthoDBiEOG6S52GD.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR002543. FtsK_dom.
    IPR018541. Ftsk_gamma.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF09397. Ftsk_gamma. 1 hit.
    PF01580. FtsK_SpoIIIE. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00843. Ftsk_gamma. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS50901. FTSK. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P21458-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKKKRKSRK KQAKQLNIKY ELNGLLCIAI SIIAILQLGV VGQTFIYLFR    50
    FFAGEWFILC LLGLLVLGVS LFWKKKTPSL LTRRKAGLYC IIASILLLSH 100
    VQLFKNLTHK GSIESASVVR NTWELFLMDM NGSSASPDLG GGMIGALLFA 150
    ASHFLFASTG SQIMAIVMIL IGMILVTGRS LQETLKKWMS PIGRFIKEQW 200
    LAFIDDMKSF KSNMQSSKKT KAPSKKQKPA RKKQQMEPEP PDEEGDYETV 250
    SPLIHSEPII SSFSDRNEEE ESPVIEKRAE PVSKPLQDIQ PETGDQETVS 300
    APPMTFTELE NKDYEMPSLD LLADPKHTGQ QADKKNIYEN ARKLERTFQS 350
    FGVKAKVTQV HLGPAVTKYE VYPDVGVKVS KIVNLSDDLA LALAAKDIRI 400
    EAPIPGKSAI GIEVPNAEVA MVSLKEVLES KLNDRPDAKL LIGLGRNISG 450
    EAVLAELNKM PHLLVAGATG SGKSVCVNGI ITSILMRAKP HEVKMMMIDP 500
    KMVELNVYNG IPHLLAPVVT DPKKASQALK KVVNEMERRY ELFSHTGTRN 550
    IEGYNDYIKR ANNEEGAKQP ELPYIVVIVD ELADLMMVAS SDVEDSITRL 600
    SQMARAAGIH LIIATQRPSV DVITGVIKAN IPSRIAFSVS SQTDSRTILD 650
    MGGAEKLLGR GDMLFLPVGA NKPVRVQGAF LSDDEVEKVV DHVITQQKAQ 700
    YQEEMIPEET TETHSEVTDE LYDEAVELIV GMQTASVSML QRRFRIGYTR 750
    AARLIDAMEE RGVVGPYEGS KPREVLLSKE KYDELSS 787
    Length:787
    Mass (Da):87,181
    Last modified:May 26, 2009 - v3
    Checksum:i87E466262101E9D0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti439 – 4402KL → NV in AAA22784. (PubMed:3129532)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17445 mRNA. Translation: AAA22784.1. Sequence problems.
    M17445 mRNA. Translation: AAA22785.1. Sequence problems.
    AL009126 Genomic DNA. Translation: CAB13553.3.
    PIRiS09411.

    Genome annotation databases

    EnsemblBacteriaiCAB13553; CAB13553; BSU16800.
    PATRICi18975171. VBIBacSub10457_1777.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17445 mRNA. Translation: AAA22784.1 . Sequence problems.
    M17445 mRNA. Translation: AAA22785.1 . Sequence problems.
    AL009126 Genomic DNA. Translation: CAB13553.3 .
    PIRi S09411.

    3D structure databases

    ProteinModelPortali P21458.
    SMRi P21458. Positions 316-706, 714-781.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P21458. 1 interaction.
    STRINGi 224308.BSU16800.

    Protein family/group databases

    TCDBi 3.A.12.1.1. the septal dna translocator (s-dna-t) family.

    Proteomic databases

    PaxDbi P21458.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13553 ; CAB13553 ; BSU16800 .
    PATRICi 18975171. VBIBacSub10457_1777.

    Organism-specific databases

    GenoListi BSU16800. [Micado ]

    Phylogenomic databases

    eggNOGi COG1674.
    HOGENOMi HOG000010003.
    OrthoDBi EOG6S52GD.

    Enzyme and pathway databases

    BioCyci BSUB:BSU16800-MONOMER.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR002543. FtsK_dom.
    IPR018541. Ftsk_gamma.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF09397. Ftsk_gamma. 1 hit.
    PF01580. FtsK_SpoIIIE. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00843. Ftsk_gamma. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS50901. FTSK. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the sporulation operon, spoIIIE, of Bacillus subtilis."
      Butler P.D., Mandelstam J.
      J. Gen. Microbiol. 133:2359-2370(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 168.
    2. "The role of the sporulation gene spoIIIE in the regulation of prespore-specific gene expression in Bacillus subtilis."
      Foulger D., Errington J.
      Mol. Microbiol. 3:1247-1255(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    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. "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 439-440.
    5. "Bacillus subtilis spoIIIE protein required for DNA segregation during asymmetric cell division."
      Wu L.J., Errington J.
      Science 264:572-575(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    6. "An in vivo membrane fusion assay implicates SpoIIIE in the final stages of engulfment during Bacillus subtilis sporulation."
      Sharp M.D., Pogliano K.
      Proc. Natl. Acad. Sci. U.S.A. 96:14553-14558(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, MUTANT SPOIIIE-73-11.
      Strain: 168 / PY79.
    7. "Role of Bacillus subtilis SpoIIIE in DNA transport across the mother cell-prespore division septum."
      Bath J., Wu L.J., Errington J., Wang J.C.
      Science 290:995-997(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ATP-BINDING, MUTAGENESIS OF LYS-473.
    8. "Role of cell-specific SpoIIIE assembly in polarity of DNA transfer."
      Sharp M.D., Pogliano K.
      Science 295:137-139(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "The membrane domain of SpoIIIE is required for membrane fusion during Bacillus subtilis sporulation."
      Sharp M.D., Pogliano K.
      J. Bacteriol. 185:2005-2008(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEMBRANE FUSION.
      Strain: 168 / PY79.
    10. "Evidence that the SpoIIIE DNA translocase participates in membrane fusion during cytokinesis and engulfment."
      Liu N.J., Dutton R.J., Pogliano K.
      Mol. Microbiol. 59:1097-1113(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MEMBRANE FUSION, SUBCELLULAR LOCATION.
      Strain: 168 / PY79.
    11. "The ATPase SpoIIIE transports DNA across fused septal membranes during sporulation in Bacillus subtilis."
      Burton B.M., Marquis K.A., Sullivan N.L., Rapoport T.A., Rudner D.Z.
      Cell 131:1301-1312(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA TRANSLOCATION, SUBUNIT, MUTAGENESIS OF ASP-584.
      Strain: 168 / PY79.
    12. "Separation of chromosome termini during sporulation of Bacillus subtilis depends on SpoIIIE."
      Bogush M., Xenopoulos P., Piggot P.J.
      J. Bacteriol. 189:3564-3572(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SEPARATION OF CHROMOSOME TERMINI.
      Strain: 168 / BR151.
    13. "FtsK and SpoIIIE: the tale of the conserved tails."
      Barre F.X.
      Mol. Microbiol. 66:1051-1055(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN.
    14. "Cell-specific SpoIIIE assembly and DNA translocation polarity are dictated by chromosome orientation."
      Becker E.C., Pogliano K.
      Mol. Microbiol. 66:1066-1079(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DNA TRANSLOCATION.
      Strain: 168 / PY79.
    15. "SpoIIIE strips proteins off the DNA during chromosome translocation."
      Marquis K.A., Burton B.M., Nollmann M., Ptacin J.L., Bustamante C., Ben-Yehuda S., Rudner D.Z.
      Genes Dev. 22:1786-1795(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 168 / PY79.
    16. "Sequence-directed DNA export guides chromosome translocation during sporulation in Bacillus subtilis."
      Ptacin J.L., Nollmann M., Becker E.C., Cozzarelli N.R., Pogliano K., Bustamante C.
      Nat. Struct. Mol. Biol. 15:485-493(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN.
      Strain: 168 / PY79.
    17. "Sporulation: SpoIIIE is the key to cell differentiation."
      Grainge I.
      Curr. Biol. 18:R871-R872(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    18. "The Bacillus subtilis SftA (YtpS) and SpoIIIE DNA translocases play distinct roles in growing cells to ensure faithful chromosome partitioning."
      Biller S.J., Burkholder W.F.
      Mol. Microbiol. 74:790-809(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    19. "SpoIIIE and a novel type of DNA translocase, SftA, couple chromosome segregation with cell division in Bacillus subtilis."
      Kaimer C., Gonzalez-Pastor J.E., Graumann P.L.
      Mol. Microbiol. 74:810-825(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN VEGETATIVE GROWTH, SUBCELLULAR LOCATION.
      Strain: 168 / PY79.
    20. "Dynamic SpoIIIE assembly mediates septal membrane fission during Bacillus subtilis sporulation."
      Fleming T.C., Shin J.Y., Lee S.H., Becker E., Huang K.C., Bustamante C., Pogliano K.
      Genes Dev. 24:1160-1172(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN SEPTAL MEMBRANE FUSION.
      Strain: 168 / PY79.

    Entry informationi

    Entry nameiSP3E_BACSU
    AccessioniPrimary (citable) accession number: P21458
    Secondary accession number(s): P21459
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: May 26, 2009
    Last modified: October 1, 2014
    This is version 108 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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

    External Data

    Dasty 3