FTSK_HELPY
ID FTSK_HELPY Reviewed; 858 AA.
AC O25722;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=HP_1090;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(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. 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; AE000511; AAD08132.1; -; Genomic_DNA.
DR PIR; B64656; B64656.
DR RefSeq; NP_207881.1; NC_000915.1.
DR RefSeq; WP_010875590.1; NC_018939.1.
DR AlphaFoldDB; O25722; -.
DR SMR; O25722; -.
DR STRING; 85962.C694_05630; -.
DR PaxDb; O25722; -.
DR EnsemblBacteria; AAD08132; AAD08132; HP_1090.
DR KEGG; hpy:HP_1090; -.
DR PATRIC; fig|85962.8.peg.1139; -.
DR eggNOG; COG1674; Bacteria.
DR OMA; CAESIRI; -.
DR PhylomeDB; O25722; -.
DR Proteomes; UP000000429; 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..858
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098262"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 532..722
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 175..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 552..557
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 858 AA; 96445 MW; 273C6384DB36B377 CRC64;
MQPMKSKKLY LALIIGVLLA FLTLSSWLGN SGLVGRFGVW FAALNKKYFG HLSFINLPYL
AWVLFLLYKT KNPFTEIVLE KTLGHLLGIL SLLFLQSSLL NQGEIGNSAR LFLRPFIGDF
GLYALITLMV VISYLILFKL PPKSVFYPYM NKTQNLLKEI YKQCLQAFSP NFSPKKEGFE
NTPSDIQKKE TKNDKEKENR KENPINENHK TPNEEPFLAI PTPYNTTLND SEPQEGLVQI
SSHPPTHYTI YPKRNRFDDL TNPTNPPLKE IKQETKEREP TPTKETLTPT TPKPIMPTLA
PIIENDNKTE NQKTPNHPKK EENPQENTQE EMIEGRIEEM IKENLKKEEK EVQNAPNFSP
VTPTSAKKPV MVKELSENKE ILDGLDYGEV QKPKDYELPT TQLLNAVCLK DTSLDENEID
QKIQDLLSKL RTFKIDGDII RTYSGPIVTT FEFRPAPNVK VSRILGLSDD LAMTLCAESI
RIQAPIKGKD VVGIEIPNSQ SQIIYLREIL ESELFQKSSS PLTLALGKDI VGNPFITDLK
KLPHLLIAGT TGSGKSVGVN AMILSLLYKN PPDQLKLVMI DPKMVEFSIY ADIPHLLTPI
ITDPKKAIGA LQSVAKEMER RYSLMSEYKV KTIDSYNEQA PSNGVEAFPY LIVVIDELAD
LMMTGGKEAE FPIARIAQMG RASGLHLIVA TQRPSVDVVT GLIKTNLPSR VSFRVGTKID
SKVILDTDGA QSLLGRGDML FTPPGANGLV RLHAPFATED EIKKIVDFIK AQKEVQYDKD
FLLEESRMPL DTPNYQGDDI LERAKAVILE KKITSTSFLQ RQLKIGYNQA ATITDELEAQ
GFLSPRNAKG NREILQNF
