ID   FTSK2_RALSO             Reviewed;         781 AA.
AC   Q8XWX9;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=DNA translocase FtsK 2;
GN   Name=ftsK2; OrderedLocusNames=RSc2341; ORFNames=RS01205;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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. Translocation stops specifically at Xer-dif sites, where FtsK
CC       interacts with the Xer recombinase, allowing activation of chromosome
CC       unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC       the direction of DNA translocation. FtsK can remove proteins from DNA
CC       as it translocates, but translocation stops specifically at XerCD-dif
CC       site, thereby preventing removal of XerC and XerD from dif (By
CC       similarity). {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 multimerise to produce a hexameric ring,
CC       contain the nucleotide binding motif and form the DNA pump. The gamma
CC       subdomain is a regulatory subdomain that controls translocation of DNA
CC       by recognition of KOPS motifs and interacts with XerD recombinase (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR   EMBL; AL646052; CAD16048.1; -; Genomic_DNA.
DR   RefSeq; WP_011002264.1; NC_003295.1.
DR   AlphaFoldDB; Q8XWX9; -.
DR   SMR; Q8XWX9; -.
DR   STRING; 267608.RSc2341; -.
DR   EnsemblBacteria; CAD16048; CAD16048; RSc2341.
DR   GeneID; 60501850; -.
DR   KEGG; rso:RSc2341; -.
DR   PATRIC; fig|267608.8.peg.2377; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_7_4; -.
DR   OMA; YKAEARD; -.
DR   Proteomes; UP000001436; 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; 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; 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..781
FT                   /note="DNA translocase FtsK 2"
FT                   /id="PRO_0000098283"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        191..781
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          414..623
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         434..439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   781 AA;  84610 MW;  D758C8D6F22578B5 CRC64;
     MARASTTPTT RTDPAALPSR IGRLLGEVRW FLLLAVTIAF LTILLSYNKA DPGWSHASQV
     DDVRNLGGRV GAWFADVLLF VFGASAYWWA LLLLRRVWRG WRELMSDERV PRAATPRVDA
     GVTWFGFALI LSASMGLEAI RMHTLHMKLP RAPGGVLGDL IGGSLQHALG FTGGTLLLLL
     MFTVGLSLFF HFSWLNLAEQ IGAGVETLFV GFKTRRENKQ DRAIGEAAKV EREEVVETRR
     VRIEEAPPVQ IVRPAAVVKS ERVEREKQQP LFVDIQDSDL PALALLDAVP PAQETVSAET
     LEFTSRLIEK KLKDFGVEVT VVAAYPGPVI TRYEIEPATG VKGSQIVNLA KDLARSLSLV
     SVRVVETIPG KNCMGLELPN PKRQAVRLAE ILGSQVYNES ASQLTMALGK DIAGKPVVAD
     LAKMPHCMVA GTTGSGKSVG INAMILSLLY KARADAVRLI LIDPKMLELS IYEGIPHLLC
     PVVTDMRQAG HALNWAVGEM ERRYKLMSKM GVRNLAGFNK KIEEAAAREE KIHNPFSLTP
     DAPEPLDKLP MIVIVIDELA DLMMVVGKKV EELIARIAQK ARAAGIHLVL ATQRPSVDVI
     TGLIKANVPT RIAFQVSSKI DSRTILDQQG AEALLGMGDM LYLAPGTGLP VRVHGAFVSD
     DEVHRVVENL KSQGEPNYIE GLLEGGTADG EGGGDGFGGG AGLAGGGAGE ADPLYDQAVD
     VVLKNRRASI SLVQRHLRIG YNRAARLLED MEKAGLVSAM SGNGNREILA PNRNGNVVEE
     E