FTSK_RICBR
ID FTSK_RICBR Reviewed; 749 AA.
AC Q1RK79;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=RBE_0154;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04235.1; -; Genomic_DNA.
DR RefSeq; WP_011476850.1; NC_007940.1.
DR AlphaFoldDB; Q1RK79; -.
DR SMR; Q1RK79; -.
DR STRING; 336407.RBE_0154; -.
DR EnsemblBacteria; ABE04235; ABE04235; RBE_0154.
DR KEGG; rbe:RBE_0154; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_5; -.
DR OMA; RDPENHH; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000001951; 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 inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..749
FT /note="DNA translocase FtsK"
FT /id="PRO_0000280966"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..749
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 391..610
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 411..416
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 749 AA; 83190 MW; 9F924B945F423F3D CRC64;
MLYYVNKFLS NSKVQAVILG IIGLATISML VSYKLDDPSF NSATTGYTNN LLGIFGSYLS
DFLYQFFGVA AFIIPLSCFI WGKNCWQQKY RKSFIRISVM LLALFSTAAL LSNFDLEFVP
SNGGGAAGII IFHFLKQFTN QLHLLLVFFT FIIFVVLFEI KFTSLSSFII KLGKFLAYKI
QTFFYNLFSQ LTLPKLFSGK ANNKIKITPS YTKPVNEKIR FTEEPKPIMA KPAPVNPIKF
FNKPTVPKIS QNDATALPPI SLLRNPENHH IKGASSSELK QKAEELLTVL NDFGVKGQII
NIGQGPVVTL YEFEPAAGTK TSRVVGLSDD IARSLSALST RIAVVPGKNV LGIELPNKQR
EFFCLKELIE TPEYQDTSTL LPLVLGKDLA GKPLIADLAK MPHLLVAGTT GSGKSVGINA
MIVSLLYRYT PEECRFIMID PKMLELSAYD GIPHLLTPVV TEPAKAVVAL KWAVKEMENR
YRMMSNIGVK NIAGYNTKIQ EAVKEGRIIE KSIQTGFDPE TGRPIYETVA MNMEKLPFIA
VIVDEMADLM LVAGKDIEML IQRLAQMARA AGIHIIMATQ RPSVDVITGV IKANFPSRIS
FKVTSKIDSR TILGEQGSEQ LLGMGDMLFM GNTSKITRVH GPFVNESEIE QITEYLKETG
TPEYISAVTE QSDEDDSSID IGDGTSDEVL YKKAVQIVRD ERKSSISYIQ RSLRIGYNKA
ANLVEKMEKE GIVSPPNHTG KREILLPER
