FTSK_BACCR
ID FTSK_BACCR Reviewed; 793 AA.
AC Q81A03;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=BC_3793;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(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 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 ---------------------------------------------------------------------------
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; AE016877; AAP10716.1; -; Genomic_DNA.
DR RefSeq; NP_833515.1; NC_004722.1.
DR RefSeq; WP_001118781.1; NC_004722.1.
DR AlphaFoldDB; Q81A03; -.
DR SMR; Q81A03; -.
DR STRING; 226900.BC_3793; -.
DR EnsemblBacteria; AAP10716; AAP10716; BC_3793.
DR KEGG; bce:BC3793; -.
DR PATRIC; fig|226900.8.peg.3910; -.
DR HOGENOM; CLU_001981_9_6_9; -.
DR OMA; FGEWYML; -.
DR Proteomes; UP000001417; 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..793
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098237"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 136..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..793
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 458..654
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 212..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 793 AA; 88406 MW; D5BFAADF1801BC1F CRC64;
MAKQKQRGTK AKARRTIKPT LYYEIVGLTL FALSIITILQ LGVVGKSFVL FFRFFFGEWY
IIGVLGVIAL SVSFVIKRGW PNLLNKRLIG FYLIVLAILM FSHITLFNLL TKDGAVQNTS
VIVSTKDNFF LEMKKGPDSV HLGGGMFGAL MFATCYFLFD EVGAYIIGII LVILGILCIT
NKHIGEVLAP VGRILRSQFQ VMQGDYKDWR AKRTAEQTEK KKTTRSTRSK RAAEQEEIIE
PMEEISIDPP IISNFTENYP VNEEEDKRIE VEQEELITSP FIEETPPIEE PKKKRGEKIV
ESLESEAQAP PMQFSNVENK DYKLPSLDIL KFPKNKQVTN ENAEIYENAR KLERTFQSFG
VKAKVTKVHR GPAVTKYEVY PDMGVKVSKI VSLSDDLALA LAAKDIRIEA PIPGKSAVGI
EVPNSEVSMV TLREVLDSKA NNHPEEKLLI GLGRDITGEA VLARLNKMPH LLVAGATGSG
KSVCINGIIV SILMRAKPHE VKLMMIDPKM VELNVYNGVP HLLTPVVTDP KKASQALKKV
VSEMERRYEL FAHSGTRNIE GYNDYIKEHN SQSEAKQPEL PYIVVIVDEL ADLMMVASSD
VEDAIMRLAQ MARAAGIHLI IATQRPSVDV ITGVIKANIP SRIAFAVSSQ TDSRTILDGG
GAEKLLGRGD MLFIPIGASK PVRVQGAFLS DDEVERVVEY VIGQQKAQYQ EDMIPQDVLD
TKQEVEDELY DEAVQLVVEM QTASVSMLQR RFRVGYTRAA RLIDAMEMNG VVGPYEGSKP
REVLINDVQE KSS
