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FTSK_LISIN
ID   FTSK_LISIN              Reviewed;         762 AA.
AC   Q92BW9;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=lin1423;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(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. 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 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; AL596168; CAC96654.1; -; Genomic_DNA.
DR   PIR; AF1610; AF1610.
DR   RefSeq; WP_010991527.1; NC_003212.1.
DR   AlphaFoldDB; Q92BW9; -.
DR   SMR; Q92BW9; -.
DR   STRING; 272626.lin1423; -.
DR   EnsemblBacteria; CAC96654; CAC96654; CAC96654.
DR   KEGG; lin:lin1423; -.
DR   eggNOG; COG1280; Bacteria.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_6_9; -.
DR   OMA; FGEWYML; -.
DR   OrthoDB; 349533at2; -.
DR   Proteomes; UP000002513; 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   Transmembrane; Transmembrane helix.
FT   CHAIN           1..762
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098268"
FT   TRANSMEM        30..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..762
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          428..624
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          741..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         448..453
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   762 AA;  84089 MW;  FF6CF486E9F025A3 CRC64;
     MATQKKKTAG RKKTSTRSKK KKSASFRLEI TGAVLIAIGI IGILQLGFVG RGFFALAEMF
     VGLLSYVLLA GSIVLGGYMV IRRKMPHLFS KRLVGVYLIV LGFLTYIHMY FIIHNLGANA
     PVVSSTWKLV LENLFRPNQV GFVGAGMIGA AITSVTYFLL DRLGTNIIAI LLIIYGFSLV
     SGISVRQFFS KITEFVRYLF SKGKAAKEKG KEVKAKRDKK KAEKLVEVEA DEVIEVSQPI
     DASKEEKTPP IISNFSSKVE QEKAPLEEKT ESDVKEKDLE MFQQESFENE IYQLPSVDIL
     EPAKVTDQSK EYDQIKVNAK KLEDTFESFG VKAKITQVHL GPAVTKYEVQ PSVGVKVSKI
     VSLSDDIALA LAAKDIRIEA PIPGKSAIGI EVANQNVAMV SLREVLENNP KNNPDEKLQI
     ALGRDISGEA MMASLDKMPH LLVAGATGSG KSVCINGIIT SILLRAKPHE VKMMMIDPKM
     VELNVYNGIP HLLAPVVTNP KKAAQALQKV VAEMERRYDL FSHTGTRNMQ GYNDYVKKHN
     ELNEEKQPEL PFIVVIVDEL ADLMMVASND VEDAITRLAQ MARAAGIHLI IATQRPSVDV
     ITGVIKANIP SRIAFAVSSS IDSRTILDMG GAEKLLGRGD MLLLPVGSSK PTRIQGAFLS
     DKEVEDVVNY VISQQKAQYN EEMIPDDIPE VEGEVTDELY HEAVELVVEM QTASVSMLQR
     KFRIGYNRAA RLIDEMEQRG VVGPHEGSKP RRVNVELPPD IE
 
 
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