FTSK_CLOTE
ID FTSK_CLOTE Reviewed; 743 AA.
AC Q895I8;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=CTC_01286;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Located at the septum. {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 form the DNA pump, and the gamma
CC subdomain is a regulatory subdomain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE015927; AAO35852.1; -; Genomic_DNA.
DR RefSeq; WP_011099514.1; NC_004557.1.
DR AlphaFoldDB; Q895I8; -.
DR SMR; Q895I8; -.
DR STRING; 212717.CTC_01286; -.
DR EnsemblBacteria; AAO35852; AAO35852; CTC_01286.
DR GeneID; 64179076; -.
DR KEGG; ctc:CTC_01286; -.
DR HOGENOM; CLU_001981_9_2_9; -.
DR OMA; NEMTRRY; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000001412; 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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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 membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..743
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098253"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 48..68
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..743
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 411..602
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 431..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 743 AA; 83169 MW; B38D130E6E53C4D5 CRC64;
MAKKKKQKTI KLDAEIKGIL FITIGVLSLI SIMSSSNSGI IGKMSKKILV FIFGLGAFIF
PFFIIFVGVC LILKKGKVTY SGKFYGIVLF ILNTLFCLHI GDIVTKGLDR SFFQGIVDIY
NSETFLHGGV ISYIVDLPLY KLFGKWGTFV IFISIYVICF ILISQISLYS IISKFKLKKE
KRRKEKNIEI KEDVQDEVKF TEIKDSEEIP EEKIINRIKI IDFIKNTNIE ENDDTKENKP
IQKGKDSNNI QGEKDINKEL EEEMSKAALK TIDYEFPSID LLNDNKSIKL KKEDKKELLN
NANKLEETLT SFGVEAKVTQ VTKGPSVTRF ELQPSVGVKV SKIVHLADDI ALNLAAQDVR
IEAPIPGKSA VGIEVPNREL TPVYLKEVLD SNEFKNCNKN LAFAIGKDIA GNCVVSDLSK
MPHLLIAGAT GSGKSVCINT LIISLIYKYS PEDVKLLMVD PKVVELNIYN DIPHLLIPVV
TEPKKAAGAL YWAVNEMTRR YKLFAETNVR NIESYNELLK KGKGVEKLPL IVIVIDELAD
LMMVCPNDIE DYIGRLAQMA RAAGMHLVIA TQRPSVDVIT GVIKANIPSR ISFAVSSQID
SRTILDMGGA EKLLGKGDML FYPSGESKPM RVQGAFISEE EVEKVVGFIK EKQCGEVEYE
DSIIDEINTS IEINNEDRDE LLEEAIKIVV DVDQASTSLL QRKLRIGYNR AARIMDQMEE
RGIISQKDGS KPRQVLISKD DIV
