FTSK_STRPQ
ID FTSK_STRPQ Reviewed; 801 AA.
AC P0DB17; Q878C9; Q8K8E8;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=SPs1535;
OS Streptococcus pyogenes serotype M3 (strain SSI-1).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=193567;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SSI-1;
RX PubMed=12799345; DOI=10.1101/gr.1096703;
RA Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y.,
RA Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H.,
RA Hattori M., Hamada S.;
RT "Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-
RT scale genomic rearrangement in invasive strains and new insights into phage
RT evolution.";
RL Genome Res. 13:1042-1055(2003).
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}.
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DR EMBL; BA000034; BAC64630.1; -; Genomic_DNA.
DR RefSeq; WP_011106874.1; NC_004606.1.
DR AlphaFoldDB; P0DB17; -.
DR SMR; P0DB17; -.
DR KEGG; sps:SPs1535; -.
DR HOGENOM; CLU_001981_9_6_9; -.
DR OMA; MTKEPEI; -.
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_0000411346"
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
