FTSK_SPOUR
ID FTSK_SPOUR Reviewed; 780 AA.
AC Q9RNV1;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=DNA translocase FtsK;
DE AltName: Full=DNA translocase SpoIIIE;
GN Name=ftsK; Synonyms=spoIIIE;
OS Sporosarcina ureae.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Planococcaceae; Sporosarcina.
OX NCBI_TaxID=1571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 13881 / BS 860;
RX PubMed=10672183; DOI=10.1046/j.1365-2958.2000.01731.x;
RA Chary V.K., Hilbert D.W., Higgins M.L., Piggot P.J.;
RT "The putative DNA translocase SpoIIIE is required for sporulation of the
RT symmetrically dividing coccal species Sporosarcina ureae.";
RL Mol. Microbiol. 35:612-622(2000).
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 Also involved in chromosome segregation into the prespore compartment
CC during sporulation. {ECO:0000250, ECO:0000269|PubMed:10672183}.
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; AF177859; AAD52663.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9RNV1; -.
DR SMR; Q9RNV1; -.
DR eggNOG; COG1674; Bacteria.
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 GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; 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 Sporulation; Transmembrane; Transmembrane helix.
FT CHAIN 1..780
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098292"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 196..780
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 445..641
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 274..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 465..470
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 780 AA; 85799 MW; CF4813EC85AA299F CRC64;
MAKKRAKKRA PAKKRQQKKQ QSQMQPLWFE ILGVVLIGIA IIMIFEFGII GRGLSAFSRF
LLGNWYVALP FLIIVQALIF MIKRQIGGYK HRIVIGCLFI LGSMLLFSHV HLFQTLYESK
VLMSNSALKE TWKVLITNDG IHDQTGTLGG GMLGAVLFAM FYSLVDSSGA TVAGVLLLLI
GIILLTGKAL IPFLVEQTPI LMNDIKKKWA AREKKSVKSP EEKRKESARS NRKSKPKPVD
TSEMEAVQEN PEPASEPIIS SFTAKIEQAT QPEIVQEKQS KAQEDSTLDP KDPVTDYPVM
GGEQENESYV LPSAKLLEPP VASDQSGEYD LIQANAKKLE KTFLSFGVKT RVTQVHLGPA
VTKYEILPDT GVKVSRIVSL ADDIALALAA SGIRIEAPIP GKSAVGIEVP NNAVAMVSLR
EVLESKENNP PEAKLLVGLG RDVTGQAMMT ELNKMPHVLI AGATGSGKSV CVNGIIMSII
MRAKPHEVKM MMIDPKMVEL NVFNGIPHLL APVVTDPRKA AQALQRVVSE MERRYELFSH
TGTRNIEGYN NHIEQWNEDH DEKHPRMPYI VVIVDELADL MMVASSDVED SITRLAQMAR
AAGIHLIIAT QRPSVDVITG IIKANIPSRI AFAVSSAIDS RTILDGAGAE KLLGRGDMLF
LPAGASKPTR IQGAFVSDEE VEAVVNFVIE QQKAQYQEEM IPTEVEVVAP HEETDELYDE
AVQMVVDMQT ASVSMIQRRF RVGYARAARI VDQMEARGVV GPPEGSKPRH VLLTKSKLEM
