FTSK1_RALSO
ID FTSK1_RALSO Reviewed; 959 AA.
AC Q8XRH0;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=DNA translocase FtsK 1;
GN Name=ftsK1; OrderedLocusNames=RSp0884; ORFNames=RS01655;
OS Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG Plasmid megaplasmid Rsp.
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=267608;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GMI1000;
RX PubMed=11823852; DOI=10.1038/415497a;
RA Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL Nature 415:497-502(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. Translocation stops specifically at Xer-dif sites, where FtsK
CC interacts with the Xer recombinase, allowing activation of chromosome
CC unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC the direction of DNA translocation. FtsK can remove proteins from DNA
CC as it translocates, but translocation stops specifically at XerCD-dif
CC site, thereby preventing removal of XerC and XerD from dif (By
CC similarity). {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 multimerise to produce a hexameric ring,
CC contain the nucleotide binding motif and form the DNA pump. The gamma
CC subdomain is a regulatory subdomain that controls translocation of DNA
CC by recognition of KOPS motifs and interacts with XerD recombinase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; AL646053; CAD18035.1; -; Genomic_DNA.
DR RefSeq; WP_011004181.1; NC_003296.1.
DR AlphaFoldDB; Q8XRH0; -.
DR SMR; Q8XRH0; -.
DR STRING; 267608.RSp0884; -.
DR EnsemblBacteria; CAD18035; CAD18035; RSp0884.
DR GeneID; 60503792; -.
DR KEGG; rso:RSp0884; -.
DR PATRIC; fig|267608.8.peg.4360; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_14_1_4; -.
DR OMA; GETWRSL; -.
DR Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; Plasmid;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..959
FT /note="DNA translocase FtsK 1"
FT /id="PRO_0000098282"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..959
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 605..814
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 122..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 224..248
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..297
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..379
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 404..427
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 625..630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 959 AA; 100247 MW; A195A2E786E3771F CRC64;
MGLGWFGISS VWLLPMVWRY VARVMAGERG LKGPGTVRIW LATLAVLCAS ASLEALTSGR
DLHGKAGGAV GRGLASLFGH MLGWTGAFLL MLGVLLWVAP MVFGHSWRQL LARLRQAGEA
PPVQADARHD EADDGLKPTA LGLGGAEQAM GSGHAGASRR HGIEAGSAWR QPAWQPPPRT
RESPPQPGEI WPLLNAQGRP EMPLPVAAQP APVPVPAPAA TPKAATQAPS SRSALRATIV
SSPFHRPQPS DGDQPPSSPE ADDAPSAPVE DAAPAISPAA EPDAPASAPP EPAEPSPPTV
DLEAVRQEAE ALLAELRGLM TPLAAAPVAS PEPEPEPEPE AETEVTPEAE AEPEAEPEAE
AEPEAEAEAE AEAEAEPEAE APAPESVAPA LQEAEAATAA EAPLPAPEPA PAIEADDAAP
PPPAVPAQKP RIVLPAVVGQ VVSNAMPAPA PAAAPVAAAP PAPPRVVDYR LPNVALLTAA
SPDTVAVPAE HLEETSHLIA QRLAEFKVPV TVAGASAGPV ITRFEVDPAI GVRGAQVVGL
MKDLARALGV TSIRVVETIP GKTCMGLELP NARRAMIRLS EVVNAPDFQS HASHLVLAMG
KDITGNPVVT DLARAPHLLV AGTTGSGKSV AVNAMILSML YKATPEDVRL IMIDPKMLEL
SVYEGIPHLL APVVTDMKQA AHALNWCVGE MEKRYRLMSA LGVRNLAGYN QKIRAAQQAG
HKVPNPFSLT PDAPEPLSTL PMIVVVIDEL ADLMMVAGKK IEELIARLAQ KARAAGIHLI
LATQRPSVDV ITGLIKANIP TRVAFQVSSK IDSRTILDQM GAETLLGQGD MLFLPPGTGY
PQRVHGAFVA DEEVHRVVEH WKQFGEPEYD EAILAGDPAE AAAGELFGEG GDAEADPLYD
EAAAFVLNTR RASISAVQRQ LRIGYNRAAR LIEQMEAAGL VSPMGRNGSR EVIAPGGGD
