SP3E_BACSU
ID SP3E_BACSU Reviewed; 787 AA.
AC P21458; P21459;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=DNA translocase SpoIIIE;
DE AltName: Full=Stage III sporulation protein E;
GN Name=spoIIIE; Synonyms=ftsK; OrderedLocusNames=BSU16800;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=3129532; DOI=10.1099/00221287-133-9-2359;
RA Butler P.D., Mandelstam J.;
RT "Nucleotide sequence of the sporulation operon, spoIIIE, of Bacillus
RT subtilis.";
RL J. Gen. Microbiol. 133:2359-2370(1987).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=2507870; DOI=10.1111/j.1365-2958.1989.tb00275.x;
RA Foulger D., Errington J.;
RT "The role of the sporulation gene spoIIIE in the regulation of prespore-
RT specific gene expression in Bacillus subtilis.";
RL Mol. Microbiol. 3:1247-1255(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION TO 439-440.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP CHARACTERIZATION.
RX PubMed=8160014; DOI=10.1126/science.8160014;
RA Wu L.J., Errington J.;
RT "Bacillus subtilis spoIIIE protein required for DNA segregation during
RT asymmetric cell division.";
RL Science 264:572-575(1994).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND MUTANT
RP SPOIIIE-73-11.
RC STRAIN=168 / PY79;
RX PubMed=10588743; DOI=10.1073/pnas.96.25.14553;
RA Sharp M.D., Pogliano K.;
RT "An in vivo membrane fusion assay implicates SpoIIIE in the final stages of
RT engulfment during Bacillus subtilis sporulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:14553-14558(1999).
RN [7]
RP FUNCTION, ATP-BINDING, AND MUTAGENESIS OF LYS-473.
RX PubMed=11062134; DOI=10.1126/science.290.5493.995;
RA Bath J., Wu L.J., Errington J., Wang J.C.;
RT "Role of Bacillus subtilis SpoIIIE in DNA transport across the mother cell-
RT prespore division septum.";
RL Science 290:995-997(2000).
RN [8]
RP FUNCTION.
RX PubMed=11778051; DOI=10.1126/science.1066274;
RA Sharp M.D., Pogliano K.;
RT "Role of cell-specific SpoIIIE assembly in polarity of DNA transfer.";
RL Science 295:137-139(2002).
RN [9]
RP FUNCTION IN MEMBRANE FUSION.
RC STRAIN=168 / PY79;
RX PubMed=12618465; DOI=10.1128/jb.185.6.2036-2041.2003;
RA Sharp M.D., Pogliano K.;
RT "The membrane domain of SpoIIIE is required for membrane fusion during
RT Bacillus subtilis sporulation.";
RL J. Bacteriol. 185:2005-2008(2003).
RN [10]
RP FUNCTION IN MEMBRANE FUSION, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=16430687; DOI=10.1111/j.1365-2958.2005.05004.x;
RA Liu N.J., Dutton R.J., Pogliano K.;
RT "Evidence that the SpoIIIE DNA translocase participates in membrane fusion
RT during cytokinesis and engulfment.";
RL Mol. Microbiol. 59:1097-1113(2006).
RN [11]
RP FUNCTION IN DNA TRANSLOCATION, SUBUNIT, AND MUTAGENESIS OF ASP-584.
RC STRAIN=168 / PY79;
RX PubMed=18160039; DOI=10.1016/j.cell.2007.11.009;
RA Burton B.M., Marquis K.A., Sullivan N.L., Rapoport T.A., Rudner D.Z.;
RT "The ATPase SpoIIIE transports DNA across fused septal membranes during
RT sporulation in Bacillus subtilis.";
RL Cell 131:1301-1312(2007).
RN [12]
RP FUNCTION IN SEPARATION OF CHROMOSOME TERMINI.
RC STRAIN=168 / BR151;
RX PubMed=17322320; DOI=10.1128/jb.01949-06;
RA Bogush M., Xenopoulos P., Piggot P.J.;
RT "Separation of chromosome termini during sporulation of Bacillus subtilis
RT depends on SpoIIIE.";
RL J. Bacteriol. 189:3564-3572(2007).
RN [13]
RP DOMAIN.
RX PubMed=17973909; DOI=10.1111/j.1365-2958.2007.05981.x;
RA Barre F.X.;
RT "FtsK and SpoIIIE: the tale of the conserved tails.";
RL Mol. Microbiol. 66:1051-1055(2007).
RN [14]
RP FUNCTION IN DNA TRANSLOCATION.
RC STRAIN=168 / PY79;
RX PubMed=18001347; DOI=10.1111/j.1365-2958.2007.05992.x;
RA Becker E.C., Pogliano K.;
RT "Cell-specific SpoIIIE assembly and DNA translocation polarity are dictated
RT by chromosome orientation.";
RL Mol. Microbiol. 66:1066-1079(2007).
RN [15]
RP FUNCTION.
RC STRAIN=168 / PY79;
RX PubMed=18593879; DOI=10.1101/gad.1684008;
RA Marquis K.A., Burton B.M., Nollmann M., Ptacin J.L., Bustamante C.,
RA Ben-Yehuda S., Rudner D.Z.;
RT "SpoIIIE strips proteins off the DNA during chromosome translocation.";
RL Genes Dev. 22:1786-1795(2008).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=168 / PY79;
RX PubMed=18391964; DOI=10.1038/nsmb.1412;
RA Ptacin J.L., Nollmann M., Becker E.C., Cozzarelli N.R., Pogliano K.,
RA Bustamante C.;
RT "Sequence-directed DNA export guides chromosome translocation during
RT sporulation in Bacillus subtilis.";
RL Nat. Struct. Mol. Biol. 15:485-493(2008).
RN [17]
RP REVIEW.
RX PubMed=18812085; DOI=10.1016/j.cub.2008.07.047;
RA Grainge I.;
RT "Sporulation: SpoIIIE is the key to cell differentiation.";
RL Curr. Biol. 18:R871-R872(2008).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19788545; DOI=10.1111/j.1365-2958.2009.06893.x;
RA Biller S.J., Burkholder W.F.;
RT "The Bacillus subtilis SftA (YtpS) and SpoIIIE DNA translocases play
RT distinct roles in growing cells to ensure faithful chromosome
RT partitioning.";
RL Mol. Microbiol. 74:790-809(2009).
RN [19]
RP FUNCTION IN VEGETATIVE GROWTH, AND SUBCELLULAR LOCATION.
RC STRAIN=168 / PY79;
RX PubMed=19818024; DOI=10.1111/j.1365-2958.2009.06894.x;
RA Kaimer C., Gonzalez-Pastor J.E., Graumann P.L.;
RT "SpoIIIE and a novel type of DNA translocase, SftA, couple chromosome
RT segregation with cell division in Bacillus subtilis.";
RL Mol. Microbiol. 74:810-825(2009).
RN [20]
RP FUNCTION IN SEPTAL MEMBRANE FUSION.
RC STRAIN=168 / PY79;
RX PubMed=20516200; DOI=10.1101/gad.1925210;
RA Fleming T.C., Shin J.Y., Lee S.H., Becker E., Huang K.C., Bustamante C.,
RA Pogliano K.;
RT "Dynamic SpoIIIE assembly mediates septal membrane fission during Bacillus
RT subtilis sporulation.";
RL Genes Dev. 24:1160-1172(2010).
CC -!- FUNCTION: Plays an essential role during sporulation. Required for the
CC translocation of the chromosomal DNA from mother cell into the
CC forespore during polar septation, for the final steps of
CC compartmentalization in the presence of trapped DNA, and for the final
CC steps of engulfment. The N-terminus mediates localization to the
CC division septum and is required for both septal membrane fusion and
CC engulfment membrane fusion. May form DNA-conducting channels across the
CC two lipid bilayers of the septum after cell division. The C-terminus
CC functions as a DNA motor that exports DNA in an ATP-dependent manner
CC from mother cell into the forespore. DNA-binding proteins are stripped
CC off the chromosome during translocation, which may play a key role in
CC reprogramming developmental gene expression in the forespore. The two
CC arms of the chromosome are simultaneously pumped into the forespore,
CC which suggests that the septum contains at least two channels, one for
CC each arm. Required for separation of chromosome termini. Also required
CC for optimal chromosome partitioning in vegetative cells, by actively
CC moving chromosomal DNA trapped within the division septum into the
CC daughter cells. {ECO:0000269|PubMed:10588743,
CC ECO:0000269|PubMed:11062134, ECO:0000269|PubMed:11778051,
CC ECO:0000269|PubMed:12618465, ECO:0000269|PubMed:16430687,
CC ECO:0000269|PubMed:17322320, ECO:0000269|PubMed:18001347,
CC ECO:0000269|PubMed:18160039, ECO:0000269|PubMed:18391964,
CC ECO:0000269|PubMed:18593879, ECO:0000269|PubMed:19788545,
CC ECO:0000269|PubMed:19818024, ECO:0000269|PubMed:20516200}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA. Assembles into
CC complexes that could contain two hexamers.
CC {ECO:0000269|PubMed:18160039}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10588743,
CC ECO:0000269|PubMed:16430687, ECO:0000269|PubMed:18391964,
CC ECO:0000269|PubMed:19788545, ECO:0000269|PubMed:19818024}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:10588743,
CC ECO:0000269|PubMed:16430687, ECO:0000269|PubMed:18391964,
CC ECO:0000269|PubMed:19788545, ECO:0000269|PubMed:19818024}.
CC Note=Localizes to the middle of the sporulation septum, then moves to
CC the forespore pole before the completion of engulfment. Delocalizes
CC after membrane fusion is complete. During sporulation, is exclusively
CC assembled on the mother-cell side of the septum. During vegetative
CC growth, assembles at the division septum when DNA is entrapped in the
CC membranes.
CC -!- DOMAIN: Consists of an N-terminal domain, followed by a linker domain,
CC and a C-terminal domain, which forms the translocation motor involved
CC in chromosome segregation. The C-terminal domain can be further
CC subdivided into alpha, beta and gamma subdomains. Specific interactions
CC between the gamma subdomain and specific SpoIIIE recognition sequences
CC (SRS) regulate the compartment-specific activation of a mother-cell
CC SpoIIIE complex. Interactions with nonpermissive SRS in the forespore
CC lead to inactivation of the complex. {ECO:0000269|PubMed:17973909,
CC ECO:0000269|PubMed:18391964}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a chromosome
CC translocation defect and aberrant compartmentalization of both sigma-F
CC and sigma-E, and fail to complete membrane fusion at the end of
CC engulfment. {ECO:0000269|PubMed:10588743}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; M17445; AAA22784.1; ALT_SEQ; mRNA.
DR EMBL; M17445; AAA22785.1; ALT_SEQ; mRNA.
DR EMBL; AL009126; CAB13553.3; -; Genomic_DNA.
DR PIR; S09411; S09411.
DR RefSeq; NP_389562.2; NC_000964.3.
DR RefSeq; WP_003245350.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P21458; -.
DR SMR; P21458; -.
DR IntAct; P21458; 1.
DR STRING; 224308.BSU16800; -.
DR TCDB; 3.A.12.1.1; the septal dna translocator (s-dna-t) family.
DR PaxDb; P21458; -.
DR PRIDE; P21458; -.
DR EnsemblBacteria; CAB13553; CAB13553; BSU_16800.
DR GeneID; 936503; -.
DR KEGG; bsu:BSU16800; -.
DR PATRIC; fig|224308.179.peg.1823; -.
DR eggNOG; COG1674; Bacteria.
DR eggNOG; COG4980; Bacteria.
DR InParanoid; P21458; -.
DR OMA; FGEWYML; -.
DR BioCyc; BSUB:BSU16800-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR018541; Ftsk_gamma.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..787
FT /note="DNA translocase SpoIIIE"
FT /id="PRO_0000098239"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..787
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 450..646
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 213..279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 470..475
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MUTAGEN 467
FT /note="G->S: In SpoIIIE-73-11; defects in DNA
FT translocation. Can complete engulfment and membrane
FT fusion."
FT MUTAGEN 473
FT /note="K->A: Abolishes ATP-binding and DNA translocation."
FT /evidence="ECO:0000269|PubMed:11062134"
FT MUTAGEN 584
FT /note="D->A: Decrease in DNA transport."
FT /evidence="ECO:0000269|PubMed:18160039"
FT CONFLICT 439..440
FT /note="KL -> NV (in Ref. 1; AAA22784)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 787 AA; 87181 MW; 87E466262101E9D0 CRC64;
MAKKKRKSRK KQAKQLNIKY ELNGLLCIAI SIIAILQLGV VGQTFIYLFR FFAGEWFILC
LLGLLVLGVS LFWKKKTPSL LTRRKAGLYC IIASILLLSH VQLFKNLTHK GSIESASVVR
NTWELFLMDM NGSSASPDLG GGMIGALLFA ASHFLFASTG SQIMAIVMIL IGMILVTGRS
LQETLKKWMS PIGRFIKEQW LAFIDDMKSF KSNMQSSKKT KAPSKKQKPA RKKQQMEPEP
PDEEGDYETV SPLIHSEPII SSFSDRNEEE ESPVIEKRAE PVSKPLQDIQ PETGDQETVS
APPMTFTELE NKDYEMPSLD LLADPKHTGQ QADKKNIYEN ARKLERTFQS FGVKAKVTQV
HLGPAVTKYE VYPDVGVKVS KIVNLSDDLA LALAAKDIRI EAPIPGKSAI GIEVPNAEVA
MVSLKEVLES KLNDRPDAKL LIGLGRNISG EAVLAELNKM PHLLVAGATG SGKSVCVNGI
ITSILMRAKP HEVKMMMIDP KMVELNVYNG IPHLLAPVVT DPKKASQALK KVVNEMERRY
ELFSHTGTRN IEGYNDYIKR ANNEEGAKQP ELPYIVVIVD ELADLMMVAS SDVEDSITRL
SQMARAAGIH LIIATQRPSV DVITGVIKAN IPSRIAFSVS SQTDSRTILD MGGAEKLLGR
GDMLFLPVGA NKPVRVQGAF LSDDEVEKVV DHVITQQKAQ YQEEMIPEET TETHSEVTDE
LYDEAVELIV GMQTASVSML QRRFRIGYTR AARLIDAMEE RGVVGPYEGS KPREVLLSKE
KYDELSS
