ID A0A1I0MPQ0_9RHOB Unreviewed; 967 AA.
AC A0A1I0MPQ0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=SAMN05444851_0187 {ECO:0000313|EMBL:SEV89903.1};
OS Aliiroseovarius sediminilitoris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Aliiroseovarius.
OX NCBI_TaxID=1173584 {ECO:0000313|EMBL:SEV89903.1, ECO:0000313|Proteomes:UP000199650};
RN [1] {ECO:0000313|EMBL:SEV89903.1, ECO:0000313|Proteomes:UP000199650}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29439 {ECO:0000313|EMBL:SEV89903.1,
RC ECO:0000313|Proteomes:UP000199650};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOJB01000001; SEV89903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0MPQ0; -.
DR STRING; 1173584.SAMN05444851_0187; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000199650; 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:UP000199650};
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..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..213
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 601..820
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 414..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 618..625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 967 AA; 103726 MW; 27F9E6FE134AEB88 CRC64;
MAYQAKQRDP IFDSNTQAVI ERRGKELLGL GLIALGVILA LILGSYSPED PGWMSATDTP
AQNALGRVGA FIASPLAVIS GLGAWSLSLI LAVWGLRLTF HVGQDRVFGR MIFAPIAVAL
CSIYASTLVP GAGWTHSFGL GGLFGDTVLG ALLAGLPVSA GLGLKVMSVV SAIAALVAVL
FVIGADRFEM QRFGHFLMVG VVMSYAAVVS LLGKGAKGAA QGAAATARQM QARQAARKEE
RFAQVKADEA YDEEFTAPPP LRAARVMRPE PPLRGASATY GEGIEEPAPT PAKPGLLNAL
FRRTLEPELV EQPTFDGDIP EGLGGEDRIR AKIASALKNR THQPAFGDPT RAEPPLARAV
ARHRRSPDPM ILNVVPPADS HQAPAQARIV PAPDMIEDDD MVVEDLMAPD AAASEPRVYT
PPHAGLSQPA KKVVQHPAPK PVQPSARAKA EAQPSLSFEE THPGYELPPL NLLANPITIE
RHHLSDEALE ENARMLETVL DDYGVKGEIV SVRPGPVVTM YELEPAPGLK ASRVIGLADD
IARSMAALSA RVSTVPGRSV IGIELPNEKR EMVSFREILS TRDFGDGNHG LPLALGKDIG
GDPIVANLAK MPHLLIAGTT GSGKSVAINT MILSLLYRLT PEDCRMIMID PKMLELSVYD
GIPHLLSPVV TDPKKAVVAL KWVVGEMEDR YRKMSKMGVR NIEGYNGRVA DTLAKGEMFE
RTVQTGFDDD TGEPIFETEE FAPEKLPYIV VVVDEMADLM MVAGKEIEAC IQRLAQMARA
SGIHLIMATQ RPSVDVITGT IKANFPTRIS FQVTSKIDSR TILGEQGAEQ LLGMGDMLYM
AGGSKITRVH GPFVSDEEVE EIVTYLKGFG APEYVGGVVE GPPDDKADNI DAVLGLNTGG
NTTGEDAQYD QAVAIVIKDR KCSTSYIQRK LGIGYNKAAR LVEQMEDEGL VSASNHVGKR
EILIPEQ
//
