FTSK_OCEIH
ID FTSK_OCEIH Reviewed; 782 AA.
AC Q8EQS7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=OB1614;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(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 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}.
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DR EMBL; BA000028; BAC13570.1; -; Genomic_DNA.
DR RefSeq; WP_011066014.1; NC_004193.1.
DR AlphaFoldDB; Q8EQS7; -.
DR SMR; Q8EQS7; -.
DR STRING; 221109.22777297; -.
DR EnsemblBacteria; BAC13570; BAC13570; BAC13570.
DR KEGG; oih:OB1614; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_6_9; -.
DR OrthoDB; 349533at2; -.
DR PhylomeDB; Q8EQS7; -.
DR Proteomes; UP000000822; 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; 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 membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..782
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098276"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 187..782
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 444..640
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 264..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 760..782
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..300
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 464..469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 782 AA; 86825 MW; 98A4A352337B05B5 CRC64;
MAAKKRKKKR KNSKQVKRLK IELVGLLLIF LAIFGSGAAA LSDGAIPGWL ENLFQFFFGI
WYFIASVFLL VTGFYLLVKR KLPDFLHRRM IGFYILLAGV LMLTHIQVLE SLLVTTENTS
IIGMSWTLFF DYVNGTGTLV QTGGGMIGAI LFTFSHYMFS ITGSKIVVVF CLLIGAIFLT
NLSIGEVASK LFARVKAVSN IAIEKWTQYQ TERRERKQQA YMDDESRQAV NESEDNMVTE
IEVSEREEPF INDFTDVAYQ NNATQATENK SPAKQAQSIK SDQEGQSDHS AEDSKDEAMP
MTARENHDYE LPMPDLLADP SYNSQQQEKS QIQATVRKLE KTFTSFGVKA KITKVHVGPA
VTKYEVYPEA GVKVSKIVNL HDDIALALAA KDIRIEAPIP GKSAVGIEVP NKEIAMVSLR
EVLDKTWSNK TSKLLYALGR DISGEAVVGE LNKMPHLLIA GATGSGKSVC VNGIITSILM
RAKPHEVKMM MIDPKKVELN VYNGIPHLLA PVVTDPKKAS RALKKVVAEM ERRYDLFSET
GTRNIEGYNE YIRKQNLASE DQQPHLPYIV VLVDELADLM MVASNDVEDS ITRLAQMARA
AGIHLIIATQ RPSVDVITGV IKANIPSRIA FSVSSATDSR TILDSGGAEK LLGRGDMLFM
PVGSSKPTRV QGAFLSDEEV ERIVDHCVEQ QKATYQEEMI PEETNEVVED VDDDLFEDAV
QLISEMQSAS VSMLQRRFRI GYTRAARLID AMEDRGIVGP YEGSKPRSVL VPKPTEEQTT
SS
