Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P21458 (SP3E_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA translocase SpoIIIE
Alternative name(s):
Stage III sporulation protein E
Gene names
Name:spoIIIE
Synonyms:ftsK
Ordered Locus Names:BSU16800
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length787 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.19 Ref.20

Subunit structure

Homohexamer. Forms a ring that surrounds DNA. Assembles into complexes that could contain two hexamers. Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein. 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. Ref.6 Ref.10 Ref.16 Ref.18 Ref.19

Domain

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. Ref.13 Ref.16

Disruption phenotype

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. Ref.6

Sequence similarities

Belongs to the FtsK/SpoIIIE/SftA family.

Contains 1 FtsK domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 787787DNA translocase SpoIIIE
PRO_0000098239

Regions

Transmembrane22 – 4221Helical; Potential
Transmembrane51 – 7121Helical; Potential
Transmembrane87 – 10721Helical; Potential
Transmembrane154 – 17421Helical; Potential
Topological domain175 – 787613Cytoplasmic Potential
Domain450 – 646197FtsK
Nucleotide binding470 – 4756ATP Probable

Experimental info

Mutagenesis4671G → S in SpoIIIE-73-11; defects in DNA translocation. Can complete engulfment and membrane fusion.
Mutagenesis4731K → A: Abolishes ATP-binding and DNA translocation. Ref.7
Mutagenesis5841D → A: Decrease in DNA transport. Ref.11
Sequence conflict439 – 4402KL → NV in AAA22784. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21458 [UniParc].

Last modified May 26, 2009. Version 3.
Checksum: 87E466262101E9D0

FASTA78787,181
        10         20         30         40         50         60 
MAKKKRKSRK KQAKQLNIKY ELNGLLCIAI SIIAILQLGV VGQTFIYLFR FFAGEWFILC 

        70         80         90        100        110        120 
LLGLLVLGVS LFWKKKTPSL LTRRKAGLYC IIASILLLSH VQLFKNLTHK GSIESASVVR 

       130        140        150        160        170        180 
NTWELFLMDM NGSSASPDLG GGMIGALLFA ASHFLFASTG SQIMAIVMIL IGMILVTGRS 

       190        200        210        220        230        240 
LQETLKKWMS PIGRFIKEQW LAFIDDMKSF KSNMQSSKKT KAPSKKQKPA RKKQQMEPEP 

       250        260        270        280        290        300 
PDEEGDYETV SPLIHSEPII SSFSDRNEEE ESPVIEKRAE PVSKPLQDIQ PETGDQETVS 

       310        320        330        340        350        360 
APPMTFTELE NKDYEMPSLD LLADPKHTGQ QADKKNIYEN ARKLERTFQS FGVKAKVTQV 

       370        380        390        400        410        420 
HLGPAVTKYE VYPDVGVKVS KIVNLSDDLA LALAAKDIRI EAPIPGKSAI GIEVPNAEVA 

       430        440        450        460        470        480 
MVSLKEVLES KLNDRPDAKL LIGLGRNISG EAVLAELNKM PHLLVAGATG SGKSVCVNGI 

       490        500        510        520        530        540 
ITSILMRAKP HEVKMMMIDP KMVELNVYNG IPHLLAPVVT DPKKASQALK KVVNEMERRY 

       550        560        570        580        590        600 
ELFSHTGTRN IEGYNDYIKR ANNEEGAKQP ELPYIVVIVD ELADLMMVAS SDVEDSITRL 

       610        620        630        640        650        660 
SQMARAAGIH LIIATQRPSV DVITGVIKAN IPSRIAFSVS SQTDSRTILD MGGAEKLLGR 

       670        680        690        700        710        720 
GDMLFLPVGA NKPVRVQGAF LSDDEVEKVV DHVITQQKAQ YQEEMIPEET TETHSEVTDE 

       730        740        750        760        770        780 
LYDEAVELIV GMQTASVSML QRRFRIGYTR AARLIDAMEE RGVVGPYEGS KPREVLLSKE 


KYDELSS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17445 mRNA. Translation: AAA22784.1. Sequence problems.
M17445 mRNA. Translation: AAA22785.1. Sequence problems.
AL009126 Genomic DNA. Translation: CAB13553.3.
PIRS09411.

3D structure databases

ProteinModelPortalP21458.
SMRP21458. Positions 316-706, 714-781.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP21458. 1 interaction.
STRING224308.BSU16800.

Protein family/group databases

TCDB3.A.12.1.1. the septal dna translocator (s-dna-t) family.

Proteomic databases

PaxDbP21458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13553; CAB13553; BSU16800.
PATRIC18975171. VBIBacSub10457_1777.

Organism-specific databases

GenoListBSU16800. [Micado]

Phylogenomic databases

eggNOGCOG1674.
HOGENOMHOG000010003.
OrthoDBEOG6S52GD.
ProtClustDBCLSK873312.

Enzyme and pathway databases

BioCycBSUB:BSU16800-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR002543. Cell_div_FtsK/SpoIIIE.
IPR018541. DNA_translocase_Ftsk_gamma.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF09397. Ftsk_gamma. 1 hit.
PF01580. FtsK_SpoIIIE. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00843. Ftsk_gamma. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS50901. FTSK. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSP3E_BACSU
AccessionPrimary (citable) accession number: P21458
Secondary accession number(s): P21459
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 26, 2009
Last modified: April 16, 2014
This is version 105 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList