FTSK_RICPR
ID FTSK_RICPR Reviewed; 744 AA.
AC Q9ZCD4;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=RP823;
OS Rickettsia prowazekii (strain Madrid E).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=272947;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Madrid E;
RX PubMed=9823893; DOI=10.1038/24094;
RA Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA Kurland C.G.;
RT "The genome sequence of Rickettsia prowazekii and the origin of
RT mitochondria.";
RL Nature 396:133-140(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. 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; AJ235273; CAA15248.1; -; Genomic_DNA.
DR PIR; H71643; H71643.
DR RefSeq; NP_221172.1; NC_000963.1.
DR RefSeq; WP_010886379.1; NC_000963.1.
DR AlphaFoldDB; Q9ZCD4; -.
DR SMR; Q9ZCD4; -.
DR STRING; 272947.RP823; -.
DR EnsemblBacteria; CAA15248; CAA15248; CAA15248.
DR GeneID; 57569945; -.
DR KEGG; rpr:RP823; -.
DR PATRIC; fig|272947.5.peg.859; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_5; -.
DR OMA; RDPENHH; -.
DR Proteomes; UP000002480; 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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..744
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098287"
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 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 200..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; 82819 MW; C8208B0A9D9E42AC CRC64;
MLFYINKILS NNKVQAVILW IIGLAIVIVL MSYNIDDPSF NSVTTEYPSN LIGIVGAYLS
DFLYQFFGLT SFIIPLACFI WGRNCWYGRY RSAFIRIFVV LLALISSSTL LSKIKLELIP
ASAGGAIGII VSNFCERFIN QLYLLLIFPT FIILVVLLEI KFTAISNFMI KLSKFLTYWI
LLFFNYVLPR LSLIGLFPIK NNDKLNITSF YQKPASGKVK FTEEASLIPA NPIKCFIKPV
CTKISQNQIA SLPPISLLCD PKNNHVKGAS SSELKQKAEE LLTVLNDFGV KGQIININQG
PVVTQYEFEP AAGTKTSRVV GLSDDIARSL SALSTRIAVI PGKNVLGIEL PNKQREFFCL
KELIETNEYQ DKSILLPLVL GKDLAGKPLI ADLAKMPHLL VAGTTGSGKS VGINAMIVSL
LYRYTPEECR FIMIDPKMLE LSAYDGIPHL LTPVVTEPSK AVIALKWAVK EMENRYRMMS
NIGVKNIAGY NAKILEAVKE NRVIERPIQT GFDPETGKPI YETVTMNMVK LPYIVVIVDE
MADLMLVSGK DIEMLIQRLA QMARAAGIHI IMATQRPSVD VITGVIKANF PSRISFKVTS
KIDSRTILGE QGSEQLLGMG DMLFMGNTSK ISRVHGPFVN EAEIAKITEY LKETSMPVYI
SAVTEQPEEN YSSIDIGDGS IDEVLYKKAV QIVRNERKSS ISYIQRSLRI GYNKAANLVE
KMEKDGIVSS PNHTGKREIL LPEM
