FTSK_RICCN
ID FTSK_RICCN Reviewed; 744 AA.
AC Q92G50;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=RC1274;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL03812.1; -; Genomic_DNA.
DR PIR; B97859; B97859.
DR RefSeq; WP_010977836.1; NC_003103.1.
DR AlphaFoldDB; Q92G50; -.
DR SMR; Q92G50; -.
DR EnsemblBacteria; AAL03812; AAL03812; RC1274.
DR KEGG; rco:RC1274; -.
DR PATRIC; fig|272944.4.peg.1465; -.
DR HOGENOM; CLU_001981_9_7_5; -.
DR OMA; RDPENHH; -.
DR Proteomes; UP000000816; 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..744
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098286"
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..744
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 386..605
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 406..411
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 744 AA; 82916 MW; 99BE4E883051B921 CRC64;
MLYYINKILS NNKVQAVILG IIGLGIVIVL TSYNIDDPSF NSVTTEYHSN LVGIFGSYLS
DCLYQFFGLA AFIIPLACFV WGRNCWYGRY RGSFIRMFVM LLALVSSSTL LSKIKLEFIP
ANAGGAIGII ASNFFERFTN QLYLLLIFFT FIILVVLFEI KFTSLSNFII KLGNFLIYRI
QSFLHNVFSR LSSIRLFPTK NNDKINITSS YQKPVSEKVK FPEEARSVPA NPIKFFSKPV
SPKISQSEIA ELPPISLLRD PEKHHVKGAS SLELKQKAEE LLTVLNDFGV KGQIININQG
PVVTQYEFEP AAGTKTSRVV GLSDDIARSL SALSTRIAVI PGKNVLGIEL PNKQREFFCL
KELIETPEYQ DKSTLLPLVL GKDLAGKPLV ADLAKMPHLL VAGTTGSGKS VGINVMIVSL
LYRYTPEECR FIMIDPKMLE LSAYDGIPHL LTPVVTEPSK AVVALKWAVK EMENRYRMMS
NIGVKNIAGY NAKILEAVKE NRIIERSIQT GFDPETGKPI YETVTMKMEK LPYIVVIVDE
MADLMLVAGK DIEMLIQRLA QMARAAGIHI IMATQRPSVD VITGVIKANF PSRISFKVTS
KIDSRTILGE QGSEQLLGMG DMLFMGSTSK ISRVHGPFVN EAEIEQITEY LKESGTPEYI
SAVTEQPEED DSGIDIGDGT SDEVLYKKAV QIVRDERKSS ISYIQRSLRI GYNKAANLVE
KMEKEGIVSP PNHTGKREIL LPER
