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P21458

- SP3E_BACSU

UniProt

P21458 - SP3E_BACSU

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Protein

DNA translocase SpoIIIE

Gene

spoIIIE

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

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

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
Complete GO annotation...

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-KW
Complete GO annotation...

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.
InParanoidiP21458.
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

        10         20         30         40         50
MAKKKRKSRK KQAKQLNIKY ELNGLLCIAI SIIAILQLGV VGQTFIYLFR
60 70 80 90 100
FFAGEWFILC LLGLLVLGVS LFWKKKTPSL LTRRKAGLYC IIASILLLSH
110 120 130 140 150
VQLFKNLTHK GSIESASVVR NTWELFLMDM NGSSASPDLG GGMIGALLFA
160 170 180 190 200
ASHFLFASTG SQIMAIVMIL IGMILVTGRS LQETLKKWMS PIGRFIKEQW
210 220 230 240 250
LAFIDDMKSF KSNMQSSKKT KAPSKKQKPA RKKQQMEPEP PDEEGDYETV
260 270 280 290 300
SPLIHSEPII SSFSDRNEEE ESPVIEKRAE PVSKPLQDIQ PETGDQETVS
310 320 330 340 350
APPMTFTELE NKDYEMPSLD LLADPKHTGQ QADKKNIYEN ARKLERTFQS
360 370 380 390 400
FGVKAKVTQV HLGPAVTKYE VYPDVGVKVS KIVNLSDDLA LALAAKDIRI
410 420 430 440 450
EAPIPGKSAI GIEVPNAEVA MVSLKEVLES KLNDRPDAKL LIGLGRNISG
460 470 480 490 500
EAVLAELNKM PHLLVAGATG SGKSVCVNGI ITSILMRAKP HEVKMMMIDP
510 520 530 540 550
KMVELNVYNG IPHLLAPVVT DPKKASQALK KVVNEMERRY ELFSHTGTRN
560 570 580 590 600
IEGYNDYIKR ANNEEGAKQP ELPYIVVIVD ELADLMMVAS SDVEDSITRL
610 620 630 640 650
SQMARAAGIH LIIATQRPSV DVITGVIKAN IPSRIAFSVS SQTDSRTILD
660 670 680 690 700
MGGAEKLLGR GDMLFLPVGA NKPVRVQGAF LSDDEVEKVV DHVITQQKAQ
710 720 730 740 750
YQEEMIPEET TETHSEVTDE LYDEAVELIV GMQTASVSML QRRFRIGYTR
760 770 780
AARLIDAMEE RGVVGPYEGS KPREVLLSKE KYDELSS
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.
InParanoidi P21458.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 109 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