ID   FTSK_STRCO              Reviewed;         917 AA.
AC   O86810;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=SCO5750; ORFNames=SC7C7.05;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA19851.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL939124; CAA19851.1; ALT_INIT; Genomic_DNA.
DR   PIR; T35683; T35683.
DR   RefSeq; NP_629875.1; NC_003888.3.
DR   AlphaFoldDB; O86810; -.
DR   SMR; O86810; -.
DR   STRING; 100226.SCO5750; -.
DR   TCDB; 3.A.12.1.4; the septal dna translocator (s-dna-t) family.
DR   GeneID; 1101192; -.
DR   KEGG; sco:SCO5750; -.
DR   PATRIC; fig|100226.15.peg.5839; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_2_2_11; -.
DR   InParanoid; O86810; -.
DR   PhylomeDB; O86810; -.
DR   Proteomes; UP000001973; 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..917
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098304"
FT   TRANSMEM        65..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        126..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        216..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        237..917
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          564..764
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          277..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          352..426
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..42
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..371
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         584..589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   917 AA;  97349 MW;  08F8861ED8662191 CRC64;
     MASRPSAAKK QPAKKAAAPA KGPVKKAAAK KAPAKRAPAK KAAARKPAPQ PAPNPTNGVY
     RLVRALWLGL AHGVGAVFRG IGQGAKNLDP AHRKDGVALL LLGVALIVAA GTWADLKGPV
     GDLVEILVTG AFGRLDLLVP ILLGAIAVRL IRHPEKPEAN GRIVIGLSAL VIGVLGQVHI
     ACGSPARSEG MQAIRDAGGL IGWGAATPLS YTMTDVLAVP LLVLLTVFGL LVVTATPVNA
     IPQRLRQLGV RLGVVHAPET DEFTNDDERY DEQWREALPA RPRKRAQPAA AEPYDPDAAE
     QEALSRRRGR PRRSAVPQPE MNRPMDAVDV AAAAAAALDG AVLHGMPPSP LVADLTQGVS
     TGDRESTTPT PTPVPAARPQ PGKLKKDATK AAGGEPAGGA VPDLTKTPLP KERDLPPRAE
     QLQLSGDITY SLPSLDSLTR GGPGKARSAA NDAIVASLTT VFTEFKVDAA VTGFTRGPTV
     TRYEVELGPA VKVERITALT KNIAYAVASP DVRIISPIPG KSAVGIEIPN TDREMVNLGD
     VLRLAESAED DDPMLVAFGK DVEGGYVMHS LAKMPHMLVA GATGSGKSSC INCLITSIMM
     RATPEDVRMI LVDPKRVELT AYEGIPHLIT PIITNPKRAA EALQWVVREM DLRYDDLAAY
     GYRHIDDFNR AVREGKVKPP EGSERELQPY PYLLVIVDEL ADLMMVAPRD VEDAIVRITQ
     LARAAGIHLV LATQRPSVDV VTGLIKANVP SRLAFATSSL ADSRVILDQP GAEKLIGKGD
     GLFLPMGANK PTRMQGAFVT EEEVATVVQH CKDQMAPVFR EDVTVGTKQK KEIDEDIGDD
     LDLLCQAAEL VVSTQFGSTS MLQRKLRVGF AKAGRLMDLM ESRSIVGPSE GSKARDVLVK
     PDELDGVLAV IRGESEG