FTSK_BRUSU
ID FTSK_BRUSU Reviewed; 854 AA.
AC Q8FYI0; G0K839;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=BS1330_I1889, BR1895;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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. Translocation stops specifically at Xer-dif sites, where FtsK
CC interacts with the Xer recombinase, allowing activation of chromosome
CC unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC the direction of DNA translocation. FtsK can remove proteins from DNA
CC as it translocates, but translocation stops specifically at XerCD-dif
CC site, thereby preventing removal of XerC and XerD from dif (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Located at the septum.
CC {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 multimerise to produce a hexameric ring,
CC contain the nucleotide binding motif and form the DNA pump. The gamma
CC subdomain is a regulatory subdomain that controls translocation of DNA
CC by recognition of KOPS motifs and interacts with XerD recombinase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; AE014291; AAN30788.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM19205.1; -; Genomic_DNA.
DR RefSeq; WP_006190925.1; NZ_KN046804.1.
DR AlphaFoldDB; Q8FYI0; -.
DR SMR; Q8FYI0; -.
DR PRIDE; Q8FYI0; -.
DR EnsemblBacteria; AEM19205; AEM19205; BS1330_I1889.
DR GeneID; 45052846; -.
DR KEGG; bms:BR1895; -.
DR KEGG; bsi:BS1330_I1889; -.
DR PATRIC; fig|204722.21.peg.2531; -.
DR HOGENOM; CLU_001981_6_1_5; -.
DR OMA; IGPANHA; -.
DR Proteomes; UP000007104; Chromosome I.
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; IPR025199; FtsK_4TM.
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; PF13491; FtsK_4TM; 1.
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 inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..854
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098244"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 118..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..854
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 489..708
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 252..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..790
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 252..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509..514
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 854 AA; 92780 MW; 2BD08EF8B5454CAC CRC64;
MRQGYSPSYP LRDERITEDR LRFANLVRRQ VYILLGLGLL SLTAMAVGAL ATWNVADPSF
SHATDNPVTN ALGYPGAVFS DLAMQFFGLA SVPALLPLAV WSLLLMIRGY IGRIARRSLA
WVGAALLFAA IASCLAVPQS WPMPIGLGGV FGDMLLRIPG FFLGGFPQGA IASAIALVLA
FPALWFCFFA SGIIGRGAEA VNPAMLSANR SADDEFADED ADNEAGGGFH FIGALTHLVL
MTTATIRRMT GLGRRRSRED DFDDMRMVRR SAETRNAPRR EPGFGAPAAD DEPPFDMDDM
DDGAPLAGQE WHDAPPPRAR KARVEQAAPS PKPGPRAQRE AQPSFLKDNG IFEMPSLHFL
AEPKLVQRDP ALSKDALEQN ARLLEGVLED FGVRGEIINV KPGPVVTLYE LEPAPGIKSS
RVIGLADDIA RSMSAIAARV AVIPGRNAIG IELPNPKREM VYLREMLASR DFEQSKAKLA
LALGKTINGE PVIADIAKMP HVLVAGTTGS GKSVAINTMI LSLLYRMTPQ ECRLIMIDPK
MLELSVYDGI PHLLTPVVTD PKKAVVALKW TVREMEDRYR KMSKVGVRNI DGFNQRVGLA
QKKGEPIART VQTGFDRNTG EAIYETEELD LEPMPYIVVI IDEMADLMMV AGKDIEGAVQ
RLAQMARAAG IHVIMATQRP SVDVITGTIK ANFPTRISFQ VTSKIDSRTI LGEQGAEQLL
GQGDMLFMAG GGRIQRVHGP FVGDDEVERI VQHLKLQGVP EYLDAITEDE DDDEGGSGPA
GTGNLEDSDD PYDQAVAVVL RDKKASTSYI QRRLGIGYNR AASIIERMED EGIVGPANHA
GKREILVPTG DDDF
