FTSK_RICFE
ID FTSK_RICFE Reviewed; 745 AA.
AC Q4UJY1;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=RF_1307;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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; CP000053; AAY62158.1; -; Genomic_DNA.
DR RefSeq; WP_011271607.1; NC_007109.1.
DR AlphaFoldDB; Q4UJY1; -.
DR SMR; Q4UJY1; -.
DR STRING; 315456.RF_1307; -.
DR EnsemblBacteria; AAY62158; AAY62158; RF_1307.
DR KEGG; rfe:RF_1307; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_5; -.
DR OMA; RDPENHH; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000008548; 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; 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;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..745
FT /note="DNA translocase FtsK"
FT /id="PRO_0000280967"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..745
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 387..606
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 407..412
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 745 AA; 82934 MW; 1808545A999F8B6C CRC64;
MLYYINKILS NNKVQAVILG IIGFAIVTVL TSYNIDDPSF NSVTTEYPSN LVGVFGSYLS
DFLYQFFGLA AFIIPLACFV WSRNCWYGRY RGSFIRIFVM LLALISSSTL LSKIKLEFIP
ANAGGAVGII ASNFFERFTN QLYLLLIFFT FIILVVLLEI KFTSLSNFII KLGKFLIYRV
QSFLHNIFSQ LSSVRLFPTK NNDKINITSS YQKPVSEKVK FTEEAKPVPA NPIKFFSKPP
AVPKISQSEI AELPPISLLR DPENHNVKGA SSSELKQKAE ELLTVLNDFG VKGHIININQ
GPVVTQYEFE PAAGTKTSRV VGLSDDIARS LSALSTRIAV IPGKNVLGIE LPNKQREFFC
LKELIETPEY QDKSTLLPLV LGKDLAGKPL IADLAKMPHL LVAGTTGSGK SVGINAMIVS
LLYRYTPEEC RFIMIDPKML ELSAYDGIPH LLTPVVTEPS KAVVALKWAV KEMENRYRMM
SNIGVKNIAG YNAKILEAVK ENRVIERSIQ TGFDPETGKP IYETVTMNME KLPYIVVIVD
EMADLMLVAG KDIEMLIQRL AQMARAAGIH IIMATQRPSV DVITGVIKAN FPSRISFKVT
SKIDSRTILG EQGSEQLLGM GDMLFMGNTS KISRVHGPFV NEAEIEKITE YLKETGTPEY
ISAVTEQPEE DDSSIDIGDG TSDEVLYKKA VQIVRDERKS SISYIQRSLR IGYNKAANLV
EKMEKEGIVS PPNHTGKREI LLPER
