ID A0A2T0WYL6_9RHOB Unreviewed; 998 AA.
AC A0A2T0WYL6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=CLV74_103379 {ECO:0000313|EMBL:PRY91790.1};
OS Donghicola tyrosinivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Donghicola.
OX NCBI_TaxID=1652492 {ECO:0000313|EMBL:PRY91790.1, ECO:0000313|Proteomes:UP000238392};
RN [1] {ECO:0000313|EMBL:PRY91790.1, ECO:0000313|Proteomes:UP000238392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100212 {ECO:0000313|EMBL:PRY91790.1,
RC ECO:0000313|Proteomes:UP000238392};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|ARBA:ARBA00024784}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRY91790.1}.
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DR EMBL; PVTQ01000003; PRY91790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T0WYL6; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000238392; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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 CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000238392};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 27..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 631..850
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 333..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 648..655
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 998 AA; 108535 MW; 89BC1FBED042FEAC CRC64;
MAYQTRQRDP LLDSSMQEMI EKRGKELFGL GLVIMGLLAL AMAVSYTPSD PSFLSVTDAP
VQNWLGQTGA SIAAPVFMIV GWGALAFAAL LVGWGLRFVF HRGADRAVPR LMLAPVWVVL
MTTYVATLVP YEGWTQDSGL GGHLGDMLLG MFLGLLPLSQ AVALKALSLL MGPGVLAMGA
FVLGFTGEEL RRGGRFVLVG LIRAYDAVMT LMGRGAGGAM AQARAFKERR AQDDVVEDYA
PAATSRVIRH DAHYEPEEEL VDDRDYDAAP LGGLRRLMPG LLRRQPEPMP DLEPELVETP
APDFDIEAPQ EDRIKARITS VVRTKLRRPV ETETPLTRGM GRRPDPLVLK PRAAAGEPPL
TAAHAAPQVQ APMATPEAPV AEMAAAAVAP VAVDPQAALD ALPQLMENYA IDSEAIAKTA
VDFRPEPVPE VDEQIEEDFD DGDYGYDDAA PAYDLPKAEP RKAVVHQPQP KPVQPSRRAM
AEAQPSLFQN RDDEYELPPL SLLRSPESVQ KLQLSNDALE ANARMLETVL DDYGVKGEIV
SVRPGPVVTM YELEPAPGLK ASRVIGLADD IARSMSALSA RVSTVPGRSV IGIELPNETR
EMVVFREILS SRAFGDHKLS LPLALGKDIG GDPVVANLAK MPHLLIAGTT GSGKSVAINT
MILSLLYKLS PEECRLIMID PKMLELSVYD GIPHLLSPVV TDPKKAVVAL KWVVAEMEER
YRKMSKMGVR NIDGYNSRVK DALSKGEMFS RTVQTGFDED SGDPVFETEH FAPEKMPYIV
VIVDEMADLM MVAGKEIEAC IQRLAQMARA SGIHLIMATQ RPSVDVITGT IKANFPTRIS
FQVTSKIDSR TILGEQGAEQ LLGMGDMLYM AGGGRIQRCH GPFVSDEEVE EIVNHLKAYG
PPEYVNGVQS GPDAEKESEL DQVLGLSTGG NTGSEDALYD QAVQIVIKDR KCSTSYIQRK
LGIGYNKAAR LVEQMEENSL VSSANHVGKR EILVPEQD
//
