ID   FTSK_LEPIC              Reviewed;         948 AA.
AC   Q72TG0;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=LIC_11061;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS   (strain Fiocruz L1-130).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=267671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fiocruz L1-130;
RX   PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA   Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA   Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA   Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA   Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA   Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA   Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA   Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA   Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA   Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA   Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT   "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT   insights into physiology and pathogenesis.";
RL   J. Bacteriol. 186:2164-2172(2004).
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; AE016823; AAS69668.1; -; Genomic_DNA.
DR   RefSeq; WP_000444199.1; NC_005823.1.
DR   AlphaFoldDB; Q72TG0; -.
DR   SMR; Q72TG0; -.
DR   PaxDb; Q72TG0; -.
DR   EnsemblBacteria; AAS69668; AAS69668; LIC_11061.
DR   GeneID; 61144384; -.
DR   KEGG; lic:LIC_11061; -.
DR   HOGENOM; CLU_001981_9_7_12; -.
DR   OMA; CFAITLQ; -.
DR   Proteomes; UP000007037; Chromosome I.
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; IPR003593; AAA+_ATPase.
DR   InterPro; IPR025199; FtsK_4TM.
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; PF13491; FtsK_4TM; 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; 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   Transmembrane; Transmembrane helix.
FT   CHAIN           1..948
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098266"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..948
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          622..816
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          389..458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        397..417
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        430..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         642..647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   948 AA;  106585 MW;  421A1EFA9443ABBC CRC64;
     MESKPKEFKP TWNLQNGKMI LPYVLLFAGI ILTLSLGSFD AGERGVEYNF FGRLGYYISY
     GMFFMFGAAS FLPGLFTIGL GSLRLVKEEF ELTNRLFSIP VFLLCYTVTL QVTGHVSTIP
     FASQGGFVGQ LLSSGLEFVF GSTGKILIHL VFYFYGLILL LNESPLHFIG RILGTAGAKY
     KEGFKSGFGK RGESLGSLFQ SAVEKFQKKE SVPPWISTNT NEKNSLNQSY SLSNPHTHSY
     ERNLGNKQPS ELQNTLHSTF GKEGKLSDFL SKVDTGPTVT SKNSRIRFQN HGAFSGNFEE
     QGKVFRFESV SSSLSEKIRE EKNFQKTPSR WEILDFRTSS FSNIISEKEP SVTLVVPSES
     EIKKEWNQTN PILQSEEIPD KFLFEEKEKV EQTDSGLENE CYEEESVDSE ENLSEEETLS
     SETSTEKDIS ENFKTSTISN SKEVSPNHTS NSSIHSLEKS EEKLELGLPF PPTTLVPEVK
     SKRSIYHVPL KSLKTTTTKI QDPLFKIEAD KVARKIEEII RQYGYESQVV SMERGPIITR
     YELTPPLGVK LGRITSLSDE LRLYLAVKNI RIVAPIPGKS TIGIEVPNSI REDVFLGDIL
     HQNLSLRPKK DLSILIGKDI SGKLVGIDLN KLPHLLVAGT TGSGKSVCLN SMISSLVVHL
     SPEEVRFIMI DPKMVELTLY EDIPHLLMPV ITDPKKATRA LAWAIQEMEA RYHSVSKLKC
     RDFKTYNEKV EQGAHRDGYK KMPYIVIFID ELADLMMVSG KDLEDAITRI TQKSRAVGIH
     LIMATQRPSV DVITGLIKAN CPARMAFHVA QKTDSKIILD QNGAESLLGK GDFLYKSPTA
     ADLIRIQSPY VSEEEIEKIV EEARKFGKPS YVDFNLDEET ESSVVDEGDE ELFEQAWEIV
     RTDRKASASY LQRRMRIGYN KAARLMELME ERGYVSPQIG SKGREILK