FTSK_LACLA
ID FTSK_LACLA Reviewed; 763 AA.
AC Q9CF25;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=LL1656; ORFNames=L0211;
OS Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=272623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL1403;
RX PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA Ehrlich S.D., Sorokin A.;
RT "The complete genome sequence of the lactic acid bacterium Lactococcus
RT lactis ssp. lactis IL1403.";
RL Genome Res. 11:731-753(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 difSL
CC recombination site, which is located within the replication terminus
CC region. Required for activation of the XerS 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 membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Located at the septum. {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; AE005176; AAK05754.1; -; Genomic_DNA.
DR PIR; H86831; H86831.
DR RefSeq; NP_267812.1; NC_002662.1.
DR RefSeq; WP_003129457.1; NC_002662.1.
DR AlphaFoldDB; Q9CF25; -.
DR SMR; Q9CF25; -.
DR STRING; 272623.L0211; -.
DR PaxDb; Q9CF25; -.
DR PRIDE; Q9CF25; -.
DR EnsemblBacteria; AAK05754; AAK05754; L0211.
DR KEGG; lla:L0211; -.
DR PATRIC; fig|272623.7.peg.1777; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_9; -.
DR OMA; MTKEPEI; -.
DR Proteomes; UP000002196; 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; 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; 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 membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..763
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098264"
FT TRANSMEM 34..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 61..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..175
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..763
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 416..613
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 668..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 763 AA; 83627 MW; D595E2E91B38598E CRC64;
MSESKKMPAK KKTTRRNTKK EQQKKAATRK MIAFFVGLLL ILFALARLGI VGVLLYNIVR
LFVGSLAIVF LLLLAGLMII SVFRKQVLKE NKRIIPAIIL TFIGLMFVFQ IRLHQGFNET
FHLIWSDLMA GRVIHFVGSG VIGALITEPA KALFSVIGVY IIAAVLWLVA IYLMIPGLFP
KMREDLHQRL AKWKEKHAEK VEAKKAAKAL AELEKKQAVA EREELPEAAE NSLFTSAPTE
IPINIPEAPF EENETESPVL AEVPLDDEPV NFSNTNNYNG NYKLPTIDLL AEVPVKNQSG
ERENVRKNIG ILEETFKSFG IGANVESAVV GPSITKYEIK LATGTKVSRV VNLSDDLALA
LAAKDIRIEA PIPGKSLVGV EIPNAEVAMV GFREMWEAGK TNPSKLLEIP LGKSLDGGIR
TFDLTRMPHL LVAGSTGSGK SVAVNGIITS ILMKALPSQV KFLMVDPKMV ELSVYNDIPH
LLIPVVTNPR KASRALQKVV DQMEERYELF SRYGVRNIAG YNEKVQRYNA ESDEKMLELP
LIVVIVDELA DLMMVASKEV EDAIIRLGQK ARAAGIHMIL ATQRPSVDVI SGLIKANVPS
RIAFAVSSGT DSRTILDTNG AEKLLGRGDM LFKPIDENHP IRLQGAFLSD DDVESVVTFI
KDQSEAQYDE SFDPGEVDES QVGTGASNTG SGDPLFEEAR NMVIMAQKAS TAQLQRALKV
GFNRASDLMN ELEAQGIVGP AKGTTPRKVL VSPDGEFIGG VEE
