ID   FTSK_CAMJE              Reviewed;         946 AA.
AC   Q0PA12; Q46089; Q9PP45;
DT   03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; Synonyms=ftsQ; OrderedLocusNames=Cj0886c;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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; AL111168; CAL35007.1; -; Genomic_DNA.
DR   PIR; F81361; F81361.
DR   RefSeq; WP_010891893.1; NC_002163.1.
DR   RefSeq; YP_002344285.1; NC_002163.1.
DR   AlphaFoldDB; Q0PA12; -.
DR   SMR; Q0PA12; -.
DR   STRING; 192222.Cj0886c; -.
DR   PaxDb; Q0PA12; -.
DR   PRIDE; Q0PA12; -.
DR   EnsemblBacteria; CAL35007; CAL35007; Cj0886c.
DR   GeneID; 905152; -.
DR   KEGG; cje:Cj0886c; -.
DR   PATRIC; fig|192222.6.peg.870; -.
DR   eggNOG; COG1196; Bacteria.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_8_1_7; -.
DR   OMA; VHEHSQQ; -.
DR   Proteomes; UP000000799; 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; 2.
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..946
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098245"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        107..946
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          620..810
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         640..645
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   946 AA;  107863 MW;  825D15A43BEAB4FD CRC64;
     MLAPGMGEWV YKANLFLFGE FAYYYPFFLF ILNYVYYKRN YKLANFTRRE LFGIGFAFFS
     SLLLFAVFYP NSGYILELAY AIFSTILGHT GSGIFALLLL LFSLVLLFPK FAKEILKIEL
     DFTYLLKVEQ AFKSLLMRVF GGENEKEDVG KSEPIVPKLN ILQDSIYGNL QINKKGETNN
     LEQIIKDSNI NASKNSITTA KENFEKLKNQ ILDETIEIDK QSLKESRSFV HEHSQQVRNF
     AQKASKMSIS LDEDFNFISE EEVDMIPERF LKPKKLEDIK QIDTNKNLDE PSYKRKNIEI
     PVSNQEVKPK IFTKELELRE NLIKKEKLEQ EYKAYQNEIL ENKVKQEIKK LEEYDAINSS
     DIIEGNKYSF NSPKTIKTET EESDKINENK NLDKADNIFE FAPIVEELNH PYIEPTPIKN
     INEIVIEEKN TLDFIQNTET KIDNEKTNDQ EIKLQKAVLA KEIAINQALL REIEQGEIEK
     PKDFTLPPLD FLANPKEHKQ EINESEIDKK IYNLLEKLRR FKIGGDVIST YVGPVVTTFE
     FRPSADVKVS RILNLQDDLT MALMAKSIRI QAPIPGKDVV GIEVPNDEIQ TIYLREILQS
     EVFKNAKSPL TIALGKDIVG NAFVTDLKKL PHLLIAGTTG SGKSVGINSM LLSLLYRNSP
     KTLRLMMIDP KMLEFSIYND IPHLLTPVIT DPKKAVNALS NMVAEMERRY RLMADAKTKN
     IENYNEKMKE LGGEKLPFIV VIIDELADLM MTAGKDVEFY IGRLAQMARA SGIHLIVATQ
     RPSVDVVTGL IKANLPSRIS YKVGQKIDSK VILDAMGAES LLGRGDCLFT PPGTSSIVRL
     HAPFASEFEI EKIVDFLKDQ QSVEYDESFL KDQQSVGVTT NESFDGEADE LYEEAKRVIL
     EDGKTSISYL QRRLKIGYNR SANIIEQLTQ NGILSEPDAK GQREIL