FTSK_LACLM
ID FTSK_LACLM Reviewed; 755 AA.
AC A2RJB8;
DT 22-FEB-2012, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=llmg_0766;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
RN [2]
RP FUNCTION IN XERS-MEDIATED RECOMBINATION, AND SUBCELLULAR LOCATION.
RC STRAIN=MG1363;
RX PubMed=17630835; DOI=10.1371/journal.pgen.0030117;
RA Le Bourgeois P., Bugarel M., Campo N., Daveran-Mingot M.-L., Labonte J.,
RA Lanfranchi D., Lautier T., Pages C., Ritzenthaler P.;
RT "The unconventional Xer recombination machinery of
RT Streptococci/Lactococci.";
RL PLoS Genet. 3:E117-E117(2007).
RN [3]
RP FUNCTION IN XERS-MEDIATED RECOMBINATION, AND DOMAIN.
RX PubMed=20542912; DOI=10.1093/nar/gkq507;
RA Nolivos S., Pages C., Rousseau P., Le Bourgeois P., Cornet F.;
RT "Are two better than one? Analysis of an FtsK/Xer recombination system that
RT uses a single recombinase.";
RL Nucleic Acids Res. 38:6477-6489(2010).
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 (By similarity). Required for activation of the XerS
CC recombinase, allowing activation of chromosome unlinking by
CC recombination. {ECO:0000250, ECO:0000269|PubMed:17630835,
CC ECO:0000269|PubMed:20542912}.
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.
CC {ECO:0000269|PubMed:17630835}.
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). The DNA motor and
CC the gamma subdomain are both required to activate XerS recombinase.
CC {ECO:0000250, ECO:0000269|PubMed:20542912}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; AM406671; CAL97370.1; -; Genomic_DNA.
DR RefSeq; WP_011834750.1; NZ_WJVF01000008.1.
DR AlphaFoldDB; A2RJB8; -.
DR SMR; A2RJB8; -.
DR STRING; 416870.llmg_0766; -.
DR EnsemblBacteria; CAL97370; CAL97370; llmg_0766.
DR KEGG; llm:llmg_0766; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_9; -.
DR OMA; MTKEPEI; -.
DR PhylomeDB; A2RJB8; -.
DR BioCyc; LLAC416870:LLMG_RS03960-MON; -.
DR Proteomes; UP000000364; 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 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..755
FT /note="DNA translocase FtsK"
FT /id="PRO_0000415773"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..755
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 408..605
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 660..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 429..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 755 AA; 82962 MW; 27CE918AAC9BB633 CRC64;
MPAKKKTTRR NTKKELQKKA ATRKMIAFFV GLLLILFALA RLGIVGILLY NIVRLFIGSL
AIILLLLVAA IMILSVFRKQ FLKENKRIIP AIILTFIGLM FVFQIRLHQG LNETFHLIWS
DLTAGRVIHF VGSGLIGAII TEPAKALFSV IGVYIIAAVL WLVAIYLMIP GLFPKMREDL
HQRLAKWKEK RAEKVEAKKA VKALKKLEEE KEIPEPQTIL PEAENSLFTS APVEIPINIP
EAPFEENENP VLEENPVDDE PVNFMNTNNY NGNYKLPTID LLAEVPVKNQ SGERENVRKN
IGILEETFKS FGIGANVESA VVGPSITKYE IKLATGTKVS RVVNLSDDLA LALAAKDIRI
EAPIPGKSLV GVEIPNAEVA MVGFREMWEA GKTNPSKLLE IPLGKSLDGG IRTFDLTRMP
HLLVAGSTGS GKSVAVNGII TSILMKALPS QVKFLMVDPK MVELSVYNDI PHLLIPVVTN
PRKASRALQK VVDQMEERYE LFSRYGVRNI AGYNEKVQRY NAESDEKMLE LPLIVVIVDE
LADLMMVASK EVEDAIIRLG QKARAAGIHM ILATQRPSVD VISGLIKANV PSRIAFAVSS
GTDSRTILDT NGAEKLLGRG DMLFKPIDEN HPVRLQGAFL SDDDVEAVVT FIKDQSEAQY
DESFDPGEVD ENQVGTGASN TGSGDPLFEE ARNMVIIAQK ASTAQLQRAL KVGFNRASDL
MNELEAQGIV GPAKGTTPRK VLVSPDGEFI GGVEE
