ID   FTSK_STRP3              Reviewed;         801 AA.
AC   P0DB16; Q878C9; Q8K8E8;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   03-AUG-2022, entry version 45.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=SpyM3_0322;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(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 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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM78929.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014074; AAM78929.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011106874.1; NC_004070.1.
DR   AlphaFoldDB; P0DB16; -.
DR   SMR; P0DB16; -.
DR   EnsemblBacteria; AAM78929; AAM78929; SpyM3_0322.
DR   KEGG; spg:SpyM3_0322; -.
DR   HOGENOM; CLU_001981_9_6_9; -.
DR   OMA; MTKEPEI; -.
DR   Proteomes; UP000000564; 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..801
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098309"
FT   TRANSMEM        31..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        89..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        155..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        178..801
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          464..660
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          720..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         484..489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   801 AA;  89292 MW;  EAF2313044DC5EED CRC64;
     MVKRNQRKKS APKKRLTKAE VEKQRAIKRM ILSVLMALLL IFAMLRLGVF GVTTYNMIRF
     LVGSLAYPFM FAWLIYLFCF KWLRQKDGMI AGVVIAFLGL LVEWHAFLFA MPRMLDQDIF
     LGTARLITRD LLALRVTEFV GGGMLGALLY KPIAFLFSNI GSYFIGFLFI LLGLFLMTPW
     DIYDVSHFVK EAVDKLAVAY QENKEKRFIK REEHRLQAEK EALEKQAQEE EKRLAELTVD
     PETGEIVEDS QSQVSYDLAE DMPKEPEILA YDSHLKDDEA SLFDQEDLAY AHEEIGAYDS
     LSALASSEDE MDMDEPVEVD FTPKTHLLYK LPTIDLFVPD KPKNQSKEKN LVRKNIKVLE
     DTFQSFGIDV KVERAEIGPS VTKYEIKPAV GVRVNRISNL ADDLALALAA KDVRIEAPIP
     GKSLIGIEVP NSEIATVSFR ELWEQSDANP ENLLEVPLGK AVNGNARSFN LARMPHLLVA
     GSTGSGKSVA VNGIISSILM KARPDQVKFM MIDPKMVELS VYNDIPHLLI PVVTNPRKAS
     KALQKVVDEM ENRYELFSKI GVRNIAGYNT KVEEFNASSE QKQIPLPLIV VIVDELADLM
     MVASKEVEDA IIRLGQKARA AGIHMILATQ RPSVDVISGL IKANVPSRMA FAVSSGTDSR
     TILDENGAEK LLGRGDMLFK PIDENHPVRL QGSFISDDDV ERIVNFIKDQ AEADYDDAFD
     PGEVSDNDPG FSGNGGAAEG DPLFEEAKAL VLETQKASAS MIQRRLSVGF NRATRLMDEL
     EEAGVIGPAE GTKPRKVLQT N