FTSK_HELPJ
ID FTSK_HELPJ Reviewed; 844 AA.
AC Q9ZM87;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=jhp_0335;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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; AE001439; AAD05914.1; -; Genomic_DNA.
DR PIR; B71944; B71944.
DR RefSeq; WP_000837232.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZM87; -.
DR SMR; Q9ZM87; -.
DR STRING; 85963.jhp_0335; -.
DR EnsemblBacteria; AAD05914; AAD05914; jhp_0335.
DR KEGG; hpj:jhp_0335; -.
DR PATRIC; fig|85963.30.peg.677; -.
DR eggNOG; COG1674; Bacteria.
DR OMA; CAESIRI; -.
DR Proteomes; UP000000804; 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 Transmembrane; Transmembrane helix.
FT CHAIN 1..844
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098263"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..844
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 518..708
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 173..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..206
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 207..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 538..543
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 844 AA; 94775 MW; 6C34822C487A360C CRC64;
MKSKKLYLAL IIGVLLAFLT LSSWLGNSGL VGRFGVWFAA INKKYFGYLS LINLPYLAWV
LFLLYRAKNP FTEIVLEKTL GHLLGILSLL FLQSSLLNQG EIGNSARLFL HPFIGDFGLY
VLIMLMVVIS YLILFKLPPK SVFYPYMNKT QSLLKEIYKQ CLQAFSPNFS LKKEGFENTP
SDSQKKETNN DKEKENLKEN PIDENHNTPN EESFLAIPTP YNTTLNNSEP QEGLVQISPH
PPTHYTIYPK RNRFDDLTNP TLKEPKQETK EREPTLKKET PTTLKPIMPI SASNTENHDK
TENHKTPNHP IKEDDLQESP QENPQKENIE ENIEEKETQN APSFSPLTLT SAKKPVMVKE
LSENKEILDG LDYGEVQKPK DYELPTTQLL NAVCLKETSL DENEIDQKIQ DLLSKLRTFK
IDGDIIRTYS GPIVTTFEFR PAPSVKVSRI LGLSDDLAMT LCAESIRIQA PIKGKDVVGI
EIPNSQSQII YLREILESEL FQKSSSPLTL ALGKDIVGNP FITDLKKLPH LLIAGTTGSG
KSVGVNAMIL SLLYKNPPDQ LKLVMIDPKM VEFSIYADIP HLLTPIITDP KKAIGALQSV
AKEMERRYSL MSEYKVKTID SYNEQAQSNG VEAFPYLIVV IDELADLMMT GGKEAEFPIA
RIAQMGRASG LHLIVATQRP SVDVVTGLIK TNLPSRVSFR VGTKIDSKVI LDTDGAQSLL
GRGDMLFTPP GTNGLVRLHA PFATEDEIKK IVDFIKAQKE VEYDKDFLLE ESRMPLDTPN
YQGDDILERA KAVILEKKIT STSFLQRQLK IGYNQAATIT DELEAQGFLS PRNAKGNREI
LQNF
