FTSK_CHLTE
ID FTSK_CHLTE Reviewed; 804 AA.
AC Q8KBK0;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=CT1787;
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=194439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS;
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M.,
RA Brenner M., Shea T.P., Parksey D.S., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J.J., Khouri H.M.,
RA White O., Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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 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 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}.
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DR EMBL; AE006470; AAM73008.1; -; Genomic_DNA.
DR RefSeq; NP_662666.1; NC_002932.3.
DR AlphaFoldDB; Q8KBK0; -.
DR SMR; Q8KBK0; -.
DR STRING; 194439.CT1787; -.
DR PRIDE; Q8KBK0; -.
DR EnsemblBacteria; AAM73008; AAM73008; CT1787.
DR KEGG; cte:CT1787; -.
DR PATRIC; fig|194439.7.peg.1621; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_10; -.
DR OMA; PKTVWLR; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000001007; 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; 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; 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 inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..804
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098249"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 89..109
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..804
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 453..650
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 206..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..729
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 474..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 804 AA; 88910 MW; F8758E140CF177E6 CRC64;
MLAALFSIAA VFGFHAEDEP YIVTLPWYEL FSSAAKAVAG TIHNPFGLFG ARVSVFFIRV
LLGYPSVMPL FGFLVLGWHL FRAKPLGPGL FFLVYTLLMA LDLSAMFGLS MLPLADLMSG
ATGRMMASFL STVIGYPGAW ALTAIIAAVL TFYMGRDFIV DTIAGVSGFF GKLLATVQAI
RAERHRKRRE KEEMRVRKKA ERMAAVLEKE QRKRDKKAQR ARKAGDASKQ KAAPFENSPE
TPAPVMDVEP APPLLNPAVS EPVVIPAEVE EIRTPEPAPV RPEEGPEMII KPGVQEAEAD
LDERALKVRT HDHVKYRFPS IDLLRRPKDE DESYDERHLA ETKDRLLEKL RIYKIDVIRI
ATTVGPRVAL FELELAPEVK ISRIKSLEND LAMAMASSSG GIRIIAPIPG KNAIGVEIPI
SKPRPVVMRS VLQVEKFKNN SMALPIVLGK SISNEVIVDD LAAMPHLLIA GATGAGKSVA
INVLLTSLLY SKKPDEVKFV LIDPKRVELK PYKLLKDHFL PKIPGMEEQI IVTDPQKAVS
ALRSVVREME HRYELLEQCG VRNIGEYNRK MKDEAMFYLV VVVDELADLM ITAGREVEEP
ITRLAQMARA VGIHLIVATQ RPSVDIITGI IKANFPSRIA FQVASKVDSR TILDVSGAEQ
LLGSGDMLFQ SAKMSKPQRI QCPYISLSEV DAITEFIGQQ PPLRAECMLP EPPSSSGNGS
SSGFDQDRGR RDSMFEEAAR LVVMHQQASV SLLQRRLRLG FSRAGRVMDQ LEQSGIVSAG
DGSKPREVLV KNEDSLELLL RNLD