ID   FTSK_STRR6              Reviewed;         767 AA.
AC   P64167; Q8DQ94; Q97RE4;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=spr0781;
OS   Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=171101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-255 / R6;
RX   PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA   Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA   DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA   Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA   Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA   McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA   Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA   Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA   Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT   "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL   J. Bacteriol. 183:5709-5717(2001).
RN   [2]
RP   FUNCTION IN XERS-MEDIATED RECOMBINATION.
RC   STRAIN=ATCC BAA-255 / R6;
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).
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   -!- 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   ---------------------------------------------------------------------------
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; AE007317; AAK99585.1; -; Genomic_DNA.
DR   PIR; E97969; E97969.
DR   RefSeq; NP_358375.1; NC_003098.1.
DR   AlphaFoldDB; P64167; -.
DR   SMR; P64167; -.
DR   STRING; 171101.spr0781; -.
DR   EnsemblBacteria; AAK99585; AAK99585; spr0781.
DR   KEGG; spr:spr0781; -.
DR   PATRIC; fig|171101.6.peg.865; -.
DR   eggNOG; COG0697; Bacteria.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_6_9; -.
DR   OMA; MTKEPEI; -.
DR   Proteomes; UP000000586; 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; 2.
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   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..767
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098307"
FT   TRANSMEM        28..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        179..767
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          433..629
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          685..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        685..702
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         453..458
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   767 AA;  84966 MW;  112F13459FDE02C0 CRC64;
     MANKNTSTTR RRPSKAELER KEAIQRMLIS LGIAILLIFA AFKLGAAGIT LYNLIRLLVG
     SLAYLAIFGL LIYLFFFKWI RKQEGLLSGF FTIFAGLLLI FEAYLVWKYG LDKSVLKGTM
     AQVVTDLTGF RTTSFAGGGL IGVALYIPTA FLFSNIGTYF IGSILILVGS LLVSPWSVYD
     IAEFFSRGFA KWWEGHERRK EERFVKQEEK ARQKAEKEAR LEQEETEKAL LDLPPVDMET
     GEILTEEAVQ NLPPIPEEKW VEPEIILPQA ELKFPEQEDD SDDEDVQVDF SAKEALEYKL
     PSLQLFAPDK PKDQSKEKKI VRENIKILEA TFASFGIKVT VERAEIGPSV TKYEVKPAVG
     VRVNRISNLS DDLALALAAK DVRIEAPIPG KSLIGIEVPN SDIATVSFRE LWEQSQTKAE
     NFLEIPLGKA VNGTARAFDL SKMPHLLVAG STGSGKSVAV NGIIASILMK ARPDQVKFMM
     VDPKMVELSV YNDIPHLLIP VVTNPRKASK ALQKVVDEME NRYELFAKVG VRNIAGFNAK
     VEEFNSQSEY KQIPLPFIVV IVDELADLMM VASKEVEDAI IRLGQKARAA GIHMILATQR
     PSVDVISGLI KANVPSRVAF AVSSGTDSRT ILDENGAEKL LGRGDMLFKP IDENHPVRLQ
     GSFISDDDVE RIVNFIKTQA DADYDESFDP GEVSENEGEF SDGDAGGDPL FEEAKSLVIE
     TQKASASMIQ RRLSVGFNRA TRLMEELEIA GVIGPAEGTK PRKVLQQ