FTSK_LEPIN
ID FTSK_LEPIN Reviewed; 948 AA.
AC Q8F1W7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=LA_3011;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS 56601).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=189518;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=56601;
RX PubMed=12712204; DOI=10.1038/nature01597;
RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT "Unique physiological and pathogenic features of Leptospira interrogans
RT revealed by whole-genome sequencing.";
RL Nature 422:888-893(2003).
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. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination (By similarity).
CC {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 form the DNA pump, and the gamma
CC subdomain is a regulatory subdomain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; AE010300; AAN50209.1; -; Genomic_DNA.
DR RefSeq; NP_713191.1; NC_004342.2.
DR RefSeq; WP_000444199.1; NC_004342.2.
DR AlphaFoldDB; Q8F1W7; -.
DR SMR; Q8F1W7; -.
DR STRING; 189518.LA_3011; -.
DR EnsemblBacteria; AAN50209; AAN50209; LA_3011.
DR GeneID; 61144384; -.
DR KEGG; lil:LA_3011; -.
DR PATRIC; fig|189518.3.peg.2989; -.
DR HOGENOM; CLU_001981_9_7_12; -.
DR InParanoid; Q8F1W7; -.
DR OMA; CFAITLQ; -.
DR Proteomes; UP000001408; Chromosome I.
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..948
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098267"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..948
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 622..816
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 389..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..417
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 642..647
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 948 AA; 106585 MW; 421A1EFA9443ABBC CRC64;
MESKPKEFKP TWNLQNGKMI LPYVLLFAGI ILTLSLGSFD AGERGVEYNF FGRLGYYISY
GMFFMFGAAS FLPGLFTIGL GSLRLVKEEF ELTNRLFSIP VFLLCYTVTL QVTGHVSTIP
FASQGGFVGQ LLSSGLEFVF GSTGKILIHL VFYFYGLILL LNESPLHFIG RILGTAGAKY
KEGFKSGFGK RGESLGSLFQ SAVEKFQKKE SVPPWISTNT NEKNSLNQSY SLSNPHTHSY
ERNLGNKQPS ELQNTLHSTF GKEGKLSDFL SKVDTGPTVT SKNSRIRFQN HGAFSGNFEE
QGKVFRFESV SSSLSEKIRE EKNFQKTPSR WEILDFRTSS FSNIISEKEP SVTLVVPSES
EIKKEWNQTN PILQSEEIPD KFLFEEKEKV EQTDSGLENE CYEEESVDSE ENLSEEETLS
SETSTEKDIS ENFKTSTISN SKEVSPNHTS NSSIHSLEKS EEKLELGLPF PPTTLVPEVK
SKRSIYHVPL KSLKTTTTKI QDPLFKIEAD KVARKIEEII RQYGYESQVV SMERGPIITR
YELTPPLGVK LGRITSLSDE LRLYLAVKNI RIVAPIPGKS TIGIEVPNSI REDVFLGDIL
HQNLSLRPKK DLSILIGKDI SGKLVGIDLN KLPHLLVAGT TGSGKSVCLN SMISSLVVHL
SPEEVRFIMI DPKMVELTLY EDIPHLLMPV ITDPKKATRA LAWAIQEMEA RYHSVSKLKC
RDFKTYNEKV EQGAHRDGYK KMPYIVIFID ELADLMMVSG KDLEDAITRI TQKSRAVGIH
LIMATQRPSV DVITGLIKAN CPARMAFHVA QKTDSKIILD QNGAESLLGK GDFLYKSPTA
ADLIRIQSPY VSEEEIEKIV EEARKFGKPS YVDFNLDEET ESSVVDEGDE ELFEQAWEIV
RTDRKASASY LQRRMRIGYN KAARLMELME ERGYVSPQIG SKGREILK
