ID FTSK_TROW8 Reviewed; 741 AA.
AC Q83MI4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=TW631;
OS Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Tropherymataceae;
OC Tropheryma.
OX NCBI_TaxID=218496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW08/27;
RX PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA Relman D.A.;
RT "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT Tropheryma whipplei.";
RL Lancet 361:637-644(2003).
CC -!- FUNCTION: Essential cell division protein that coordinates cell
CC division and chromosome segregation. The N-terminus is involved in
CC assembly of the cell-division machinery. The C-terminus functions as a
CC DNA motor that moves dsDNA in an ATP-dependent manner towards the dif
CC recombination site, which is located within the replication terminus
CC region. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Located at the septum. {ECO:0000250}.
CC -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for the
CC localization to the septal ring and is required for cell division,
CC followed by a linker domain, and a C-terminal domain, which forms the
CC translocation motor involved in chromosome segregation. The C-terminal
CC domain can be further subdivided into alpha, beta and gamma subdomains.
CC The alpha and beta subdomains form the DNA pump, and the gamma
CC subdomain is a regulatory subdomain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; BX251412; CAD67295.1; -; Genomic_DNA.
DR RefSeq; WP_011096573.1; NC_004551.1.
DR AlphaFoldDB; Q83MI4; -.
DR SMR; Q83MI4; -.
DR GeneID; 67388410; -.
DR KEGG; tws:TW631; -.
DR HOGENOM; CLU_001981_2_3_11; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..741
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098314"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..741
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 390..587
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 200..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 741 AA; 80531 MW; D208141A4E61A1E7 CRC64;
MSAKKSYLKV WRGLAGAAGS CARVFSKKSL ARRDRRDQLP FALFLFGLVG AVFQWFLYGN
WLSGIVSEYT VAAFFGGFSI VLPILLIGFS IWLFRNPQKT HDNIRVSIGL FMFSSFSAAF
LHFSAGFPYP SSGIRILSTA GGIIGWLVGL PLTTLPSYLA KTVCIIFIVL SVSVISKTPI
SKIVRVIFRY AKWLFNSDSV KTSPNSSVSS SSEHQELTGR DMPDTAGDNR HDETVTVLSG
TSLTGSPVSE YRGESSDYAL PSLDILNSYP PVKHDDAENE KVITALSGVL RQFSVNARFS
GFSRGPTVTQ YELELGEGVK VERIIALTKN ISYAVASDKV SILSPIPGKS AIGIEIPNKK
RELVALGSVL QSIHPDAHPM TVGLGKDSSG GFVLTNLTTM PHLLVAGATG SGKSSFVNSM
ITSILLRAHP SQVRLVLIDP KRVELAIYSG VPHLITPIVT DPKKASEVLQ WVVKEMERRY
DDLASFGFRH IDDFNLAVRA KKIASDSREL TPYPYLLVIV DELADLMLVA AKDVEESIVR
ITQLARASGI HIVLATQRPS VNVVTGLIKA NVPSRLAFAV SSLVDSRVIL DRPGAEKLVG
QGDGLFLPIS AGKPIRIQSS WVTENEILRV VEYVKSQAHP DYYVLEVQNQ GNIDSHIGDD
MPLLLKATEL VINSQLGSTS MLQRKLRVGF AKAGRLMDLM ESMGIVGPGQ GSKAREVLVT
PQDLDSTLAR ISASVSDSKL D
//
