FTSK_TREPA
ID FTSK_TREPA Reviewed; 799 AA.
AC O83964;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=TP_0999;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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}.
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; AE000520; AAC26587.1; -; Genomic_DNA.
DR PIR; H71255; H71255.
DR RefSeq; WP_010882443.1; NC_021490.2.
DR AlphaFoldDB; O83964; -.
DR SMR; O83964; -.
DR STRING; 243276.TPANIC_0999; -.
DR EnsemblBacteria; AAC26587; AAC26587; TP_0999.
DR GeneID; 57879510; -.
DR KEGG; tpa:TP_0999; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_11_2_12; -.
DR OMA; IYGEKCY; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000000811; 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 inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..799
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098313"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 470..662
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 167..208
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 490..495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 799 AA; 86606 MW; 009E39B56A82DE67 CRC64;
MERSPLPRII ALTFGTLLFV SAVLLTLSTF LPLFTLHRAS HWFFVPGTLL YETYAFSSLL
VPLLLLHTAL LLFVGGRSLR AESALVAFPL LFITAVCGEH GLYALRRALA ARSISPSTRG
GIDIVCVLCL LALLGAELYA ALIYGERCYV WFHARIPRDF IADGFQDPSF PPSTADHPDT
VSPPPAPSCA TADVQTPEAS APPEGQFSTE VPLQGGEFLI SEAEVQPATQ VAACGGVSTP
TALAPSVPSQ APFPLLPAPG LIQSNLPSDV HAPASPGSLP SVIPAQAPCV MALSPISAPS
VAPAETLIPA QDDEQGPPRP IPASAAPLRH PCRGYQVPYD LLDQYSEDTY EGIDELTKNL
ALLLEETFSE FNIRVEITGI KKGPVVTMFE LLPPPGIKLS KITNLQDNVA LKLAASSVRI
VAPIPGKHAI GVEVPNKKRS LVTFKELLHT RTAGSNRMAI PVILGKDVTG EPQVIDLAQT
PHLLIAGATG SGKSVCVNAL ILSILYHKCP DETKLLLIDP KIVELKLYND IAHLLTPVIT
EPKRALQALQ YILCEMERRY ALLEQLECRD IKTYNKKIQE KSIATQPLPF IVIIIDEFAD
LMVASGKELE TSVARLCAMS RAVGIHLVLA TQRPSIDVIT GLIKANIPSR IAFMVSSKMD
SRIILDEMGA EKLLGRGDML YMNPSQSFPT RIQGAYVSER ELARVIAHVR AWGTPEYLDE
EIFFDDDDAS ISGNFVDESD PLYEQAVQVV QYAGKASTSY VQRKLKIGYN RAARLIEEME
ARGVVGPPNG SKPRDVLRS