FTSK_ALKHC
ID FTSK_ALKHC Reviewed; 789 AA.
AC Q9KA95;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; Synonyms=spoIIIE; OrderedLocusNames=BH2395;
OS Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS / JCM 9153 / C-125) (Bacillus halodurans).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX NCBI_TaxID=272558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT and genomic sequence comparison with Bacillus subtilis.";
RL Nucleic Acids Res. 28:4317-4331(2000).
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; BA000004; BAB06114.1; -; Genomic_DNA.
DR PIR; C83949; C83949.
DR RefSeq; WP_010898548.1; NC_002570.2.
DR AlphaFoldDB; Q9KA95; -.
DR SMR; Q9KA95; -.
DR STRING; 272558.10175015; -.
DR PRIDE; Q9KA95; -.
DR EnsemblBacteria; BAB06114; BAB06114; BAB06114.
DR KEGG; bha:BH2395; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_6_9; -.
DR OMA; FGEWYML; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000001258; 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..789
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098238"
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 173..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 452..648
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 226..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..243
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472..477
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 789 AA; 87422 MW; 3CA32BC2F43EEBD1 CRC64;
MAKRKKKKKV AWQSQLTFEL VGLGILVIAV VALAQLGTVG ETLVRLFRFF LGEWYAVLSI
ALLVAALYIM VKREKPPLWS RRIGGLYLML LSALLFSHVG LFGQLQGNEG FSDQSVIRNT
WNLFWLDMYG EVQHSDLGGG MIGAIAYAAS HFLFADGGTL FLCFILFMAG LILLTGHSIT
DLFGKAIRRT YLWVVDFIKG TWNEWKQFRK ESKEKLEQDR KLLKERKEKK AAKRSRNEDP
AQEENDQPLE IVDFSQRVSH EAKNDATVKQ QVKPAKQEDQ VSKEAPEEDK LASQGQEGEE
MPTVSLATAV TPNDDYQLPT IELLKLPNNP NQSMEKRLLH KNAEKLRKTL ESFGVKAHVS
KVHLGPAVTK YEVNPHVGVK VSRIVNLADD LALALAAKDI RIEAPIPGKS AIGIEVPNQE
VAIVTLREVL DSPQAKADRN VLSVGLGRDI SGEPVFAPLN KMPHLLVAGA TGSGKSVCIN
GIITSILLKA KPHEVKLMMI DPKMVELNVY NGIPHLLTPV VTEPKKASQA LKKVVAEMER
RYDLFSHSGT RNIEGYNEMI TRQNEKEDAK QPTLPYIVVI VDELADLMMV ASGDVEDSIA
RLAQMARAAG IHMILATQRP SVDVITGVIK ANIPSRIAFG VSSQTDSRTI LDTGGAEKLL
GRGDMLYLPM GATKPTRVQG AFLSDEEVET IVEFVVAQQK AQYAEEMTPT EETKVTEKVD
DELYDDAVNL VIEMNSASVS MLQRRFRIGY TRAARLIDEM EARGIVGPYE GSKPREVLVQ
AQDDEASSH
