ID   FTSK_ECO57              Reviewed;        1342 AA.
AC   Q8X5H9;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=Z1235, ECs0975;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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; AE005174; AAG55377.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34398.1; -; Genomic_DNA.
DR   PIR; E85614; E85614.
DR   PIR; G90750; G90750.
DR   RefSeq; NP_309002.1; NC_002695.1.
DR   RefSeq; WP_000076999.1; NZ_SEKU01000006.1.
DR   AlphaFoldDB; Q8X5H9; -.
DR   SMR; Q8X5H9; -.
DR   STRING; 155864.EDL933_1154; -.
DR   EnsemblBacteria; AAG55377; AAG55377; Z1235.
DR   EnsemblBacteria; BAB34398; BAB34398; ECs_0975.
DR   GeneID; 917727; -.
DR   KEGG; ece:Z1235; -.
DR   KEGG; ecs:ECs_0975; -.
DR   PATRIC; fig|386585.9.peg.1092; -.
DR   eggNOG; COG1178; Bacteria.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_0_2_6; -.
DR   OMA; DPFWKPG; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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..1342
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098258"
FT   TOPO_DOM        1..24
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   TRANSMEM        25..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   TOPO_DOM        45..74
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   TRANSMEM        75..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   TOPO_DOM        99..115
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   TRANSMEM        116..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   TOPO_DOM        133..162
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   TRANSMEM        163..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   TOPO_DOM        180..1342
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P46889"
FT   DOMAIN          987..1200
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          345..386
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          576..862
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..473
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..667
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        737..799
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        800..822
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         1007..1012
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1342 AA;  148098 MW;  F52A432278548465 CRC64;
     MSQEYTEDKE VTLTKLSSGR RLLEALLILI VLFAVWLMAA LLSFNPSDPS WSQTAWHEPI
     HNLGGMPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSSDENIDYF AVSLRIIGVL
     ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIALLCV WAAGLTLFTG
     WSWVTIAEKL GGWILNILTF ASNRTRRDDT WVDEDEYEDD EEYEDENHGK QHESRRARIL
     RGALARRKRL AEKFINPMGR QTDAALFSGK RMDDDEEITY TARGVAADPD DVLFSGNRAT
     QPEYDEYDPL LNGAPITEPV AVAAAATTAT QSWAAPVEPV TQTPPVASVD VPPSQPTVAW
     QPVPGPQTGE PVIAPAPEGY PQQSQYAQPA VQYNEPLQQP VQPQQPYYAP AAEQPAQQPY
     YAPAPEQPVA GNAWQAEEQQ STFAPQSTYQ TEQTYQQPAA QEPLYQQPQP VEQQPVVEPE
     PVVEETKPAR PPLYYFEEVE EKRAREREQL AAWYQPIPEP VKEPEPIKSS LKAPSVAAVP
     PVEAAAAVSP LASGVKKATL ATGAAATVAA PVFSLANSGG PRPQVKEGIG PQLPRPKRIR
     VPTRRELASY GIKLPSQRAA EEKAREAQRN QYDSGDQYND DEIDAMQQDE LARQFAQTQQ
     QRYGEQYQHD VPVNAEDADA AAEAELARQF AQTQQQRYSG EQPAGANPFS LDDFEFSPMK
     ALLDDGPHEP LFTPIVEPVQ QPQQPVAPQQ QYQQPQQPVA PQPQYQQPQQ QVAPQPQYQQ
     PQQPVAPQQQ YQQPQQPVAP QPQYQQPQQP VAPQPQYQQP QQPVAPQPQD TLLHPLLMRN
     GDSRPLHKPT TPLPSLDLLT PPPSEVEPVD TFALEQMARL VEARLADFRI KADVVNYSPG
     PVITRFELNL APGVKAARIS NLSRDLARSL STVAVRVVEV IPGKPYVGLE LPNKKRQTVY
     LREVLDNAKF RDNPSPLTVV LGKDIAGEPV VADLAKMPHL LVAGTTGSGK SVGVNAMILS
     MLYKAQPEDV RFIMIDPKML ELSVYEGIPH LLTEVVTDMK DAANALRWCV NEMERRYKLM
     SALGVRNLAG YNEKIAEADR MMRPIPDPYW KPGDSMDAQH PVLKKEPYIV VLVDEFADLM
     MTVGKKVEEL IARLAQKARA AGIHLVLATQ RPSVDVITGL IKANIPTRIA FTVSSKIDSR
     TILDQAGAES LLGMGDMLYS GPNSTLPVRV HGAFVRDQEV HAVVQDWKAR GRPQYVDGIT
     SDSESEGGAG GFDGAEELDP LFDQAVQFVT EKRKASISGV QRQFRIGYNR AARIIEQMEA
     QGIVSEQGHN GNREVLSPPP FD