ID   FTSK_BORBU              Reviewed;         787 AA.
AC   O51272;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=BB_0257;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
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 inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=Located at the septum.
CC       {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; AE000783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; A70132; A70132.
DR   RefSeq; WP_023591458.1; NC_001318.1.
DR   RefSeq; YP_008853940.1; NC_001318.1.
DR   PRIDE; O51272; -.
DR   PATRIC; fig|224326.49.peg.656; -.
DR   OMA; WIYLNYV; -.
DR   Proteomes; UP000001807; 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   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 1.
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; SM00843; Ftsk_gamma; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS50901; FTSK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW   Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..787
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098241"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        109..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        130..787
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          459..651
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         479..484
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   787 AA;  90268 MW;  1CE0526BD866A6B3 CRC64;
     MKDFYQYFQF LFFFMLSVIS FSLFVALTPL SNVFVFFVFN LLGQILLNVF SFLSFYLIVY
     PIVNWYAYKK HIFTKRFIFN WNYTVILFFT LIFLIKINSN VEKSYFIKIF LINFGIVLGN
     FFIFTLLILE FVVWIYLNYV FFKDVNFILD TFKFLEFKIK ILFENILSYF PFSNSLDVKK
     DIKVYGDSVD DLKDSQVFDE KKNIINDEEY QALWSFSAFL RNNKKPSNIN LDKTIFEGSD
     LKEASSLNKD ILNENALNLD ENVDEIDESC EYKYLDNLED NKLVISGKVK ACEIRTKGII
     SQVAISHVYN ENVALNKKND SYVIDISVFD QKEIKNDVED IEYDKEIQKQ SMILQETLKE
     FNINAKLIDI IKGPVVTMYA VRPDKGIKLS KITSISDNIA LRLAAIRVRI IAPIPGREAV
     GIEIPNKRRE FILISEIIDS KEFRGDFRIP FALGKEISGE NIVFDLVNSP HLLIAGATGA
     GKSVCVNSLI ASIIFSKSPD EVKLIMIDPK IVELKLFNDI PHLLTPVITD VKRALEALRW
     CLDEMERRYV LLDNLLVRDI SSYNKKIKDE NLNLMILPYL VIIIDEFADL ILSARKDLEN
     LISRLAAMAR AVGIHLVLAT QRPSVDVITG VIKANFPSRI SFMVASSMDS RIILGSSGAE
     KLLGKGDMLY ISSLNPFPXR IQGGFLKERE VYRLVEEVKK FGSPNYIDDE IFIDSVKEPD
     LVALGPSDEP MFDEALEIVK TTRKASASYL QRRLKIGYNR AARIIEIMED MGYVGPVNGS
     KPREVLI