FTSK_COREF
ID FTSK_COREF Reviewed; 946 AA.
AC Q8FPC1;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=CE1861;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(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 -!- SEQUENCE CAUTION:
CC Sequence=BAC18671.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC18671.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q8FPC1; -.
DR SMR; Q8FPC1; -.
DR STRING; 196164.23493702; -.
DR EnsemblBacteria; BAC18671; BAC18671; BAC18671.
DR KEGG; cef:CE1861; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_2_1_11; -.
DR Proteomes; UP000001409; 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 membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..946
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098254"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 212..946
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 533..746
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 898..946
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..56
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 566..571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 946 AA; 100972 MW; 68CC9D0CB3A06C21 CRC64;
MTRSLGDLAR GRGDDADDFD DFDDFEEEIS TKPKARATTR RSTRASTEDV YEEDGTDSPP
RTSSWGRAGT FMDEHADGIA LTLVGIAIVL GAAVWLGVGG PVGTFIADIV HLTIGAGAWV
LPVALIAAAV ALMLNYTPDP QSRTRVGIGG SIILLCMLGL IHLFAGNPAE WAGRKNAGGA
IGAWVGTPLE LGFSVYLAVP ILFLILFYGA LKTTGITIRE FGGFVTGFFG FGAGAEDDDE
EGDDLYGHVD REIETRASGR ALPAAEPRPT RVTPRRTTSS TPRRAAASLD RYPADEPGTP
PGPPPSVAPT GSRERKQTEA STSIEPALFP EPERRKPSVS ETDEFPAVKA PETPAAEAPA
PAKDSARDAV AASRENLRQA MIQRSGMDPQ GPPKEEPEDN PGVVVSDGDS TYVLPSADLL
IPGAPAKTHS ETNDRIIEAI TDVFREFNVD AAVTGFSRGP TVTRYEIELG PGVKVSKITN
LQSNIAYAVA TENVRLLTPI PGKSAVGIEV PNADREMVRL GDVLNAPATV DNLDPMLVGL
GKDIEGDFVS YSVQKMPHLL VAGSTGSGKS AFVNSLLVSL LTRATPEEVR LILVDPKMVE
LTPYEGIPHL ITPIITQPKK AAAALQWLVE EMEQRYMDMK QTRVRHIKDF NRKIKSGEIE
TPLGSKREYR AYPYIICVVD ELADLMMTAP KEIEESIVRI TQKARAAGIH LVLATQRPSV
DVVTGLIKTN VPSRLAFATS SLTDSRVILD QGGAEKLIGM GDALFIPQGA GKPQRIQGAF
VTDEEIQAVV EAAKVQAEPD YTDGVTEDKG GDSKKIDADI GDDLDDLLEA VELVVTSQIG
STSMLQRKLR IGFAKAGRLM DLMETRGVVG PSEGSKAREV LVKPEELDTI LWMLKGADPA
DAPKEEQWGD DGYAEPVGEG PGDGSDDSSS SDGTTVVRAN PAGGVF
