ID A0A1I7ELN7_9BURK Unreviewed; 771 AA.
AC A0A1I7ELN7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:SFU24791.1};
GN ORFNames=SAMN05192563_1029102 {ECO:0000313|EMBL:SFU24791.1};
OS Paraburkholderia aspalathi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1324617 {ECO:0000313|EMBL:SFU24791.1, ECO:0000313|Proteomes:UP000198844};
RN [1] {ECO:0000313|EMBL:SFU24791.1, ECO:0000313|Proteomes:UP000198844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27731 {ECO:0000313|EMBL:SFU24791.1,
RC ECO:0000313|Proteomes:UP000198844};
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 -!- 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; FPBH01000029; SFU24791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7ELN7; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000198844; 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: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; 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; 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 26..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 412..621
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 680..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 429..436
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 771 AA; 83529 MW; 67648C22F72DEA55 CRC64;
MAKAPYSASA QALPHRMSRL FTEIRWILQV ALGVFLLMAL VSYSRHDPSW THAAQVDHIA
NWAGRVGAWT SDILLLLFGL SAYWWIVLLG RHISANYRRI TRHEELQEDA PRDAGWLADA
FAFMLVLLAC DGIEALRMWS LKVQLPRAPG GVIGEAVARG ISHALGFTGG TLALLIVLGI
GLSLYFRFSW LSVSEKVGES IISAVTFAKL RREAGRDRKL GEAAAVKREG KVEKGRVRIE
EHEPVMIVPP IVTPAKSERV EKERQVPLFT DLPGDSTLPP ISLLDAAPAA QETISADTLE
FTSRLIEKKL KDFGVEVSVV AAYPGPVVTR YEIEPATGVK GSQIVGLAKD LARSLSLVSI
RVVETIPGKN FMALELPNQR RQTVSLSEIL GSAVYADAAS PLTMGLGKDI GGKPVCADLA
KMPHLLVAGT TGSGKSVGIN AMILSLLYKA SADQVRMILI DPKMLEMSVY EGIPHLLCPV
VTDMRQAGHA LNWAVAEMER RYKLMSKLGV RNLAGYNNKI DEAAKRDEKL PNPFSLTPDD
PEPLSRLPNI VVVIDELADL MMVVGKKVEE LIARIAQKAR AAGIHLILAT QRPSVDVITG
LIKANVPTRM AFQVSSKIDS RTILDQQGAE SLLGMGDMLY LPPGSGLPVR VHGAFVSDEE
VHRVVDKLKE QGEPNYIEGI LEGGVTGEGD EGSAGAGGSG SSDGEADPLY DQAVDVVLKN
RRASISLVQR HLRIGYNRAA RLLEQMENSG VVSAMSSNGN REILAPAREA E
//