ID V9WPN9_9RHOB Unreviewed; 1053 AA.
AC V9WPN9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=Gal_03388 {ECO:0000313|EMBL:AHD11107.1};
OS Phaeobacter gallaeciensis DSM 26640.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Phaeobacter.
OX NCBI_TaxID=1423144 {ECO:0000313|EMBL:AHD11107.1, ECO:0000313|Proteomes:UP000018782};
RN [1] {ECO:0000313|EMBL:AHD11107.1, ECO:0000313|Proteomes:UP000018782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 26640 {ECO:0000313|EMBL:AHD11107.1,
RC ECO:0000313|Proteomes:UP000018782};
RA Frank O., Petersen J., Goeker M., Klenk H.-P., Rohde M., Scheuner C.;
RT "Complete genome sequence of the Phaeobacter gallaeciensis type strain CIP
RT 105210T.";
RL Submitted (DEC-2013) 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 ---------------------------------------------------------------------------
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; CP006966; AHD11107.1; -; Genomic_DNA.
DR RefSeq; WP_024098711.1; NZ_AOQA01000011.1.
DR AlphaFoldDB; V9WPN9; -.
DR GeneID; 31847741; -.
DR KEGG; pgd:Gal_03388; -.
DR PATRIC; fig|1423144.3.peg.3394; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_6_0_5; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000018782; Chromosome.
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:UP000018782};
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 145..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 687..906
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 472..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..496
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 704..711
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1053 AA; 112934 MW; 171C79119864ED4F CRC64;
MAFQTRSRDP LLDSTMQAAI EKRGKELIGV LLIGLGLMVA LMIGSYSADD PNWMVSTDAP
VQNLLGRTGA SVAFILITLF GKASWAIALF LSVWGGRCIL HRGEDRFLWP LLLSLPWLLL
VSLHLETLVP SEAWKSAHTF GLGGMIGYTF LGMLLALLPV GLIFLVKFLS LLTALGMVSL
GATVLGFTRP EVTRGLRFVL VGLILIYGAI AGLLGRGAAS GMQAALSYRS RRAERTAAAV
AMADVVDSAE TDPQMFEPMD FDDAPMAAPP LGAPSLGPAA APHARVEPAF EAAQEDAAEP
VKEKTGLFAR VPNLIRRAEP VMPEPELVEP TLSDLDAAAD LGDLPGDERI AEKIASAVRV
RRAADVAPEV DFPLTKGRGR RPEPLIFNPS QAVDGLPPEP PLTGASLDAM DAAMGGIPSL
PPAPETGFSA EIDPHRDYDA ATYDHPAATS SELQHDSSPE FVDHVASEDL PHAPAVTSGA
GQVLRRTPQT AQAVPGTPAN AAPVTPPVTL PVAEPRRAVV EQPVRKQPQP STRAKAEAQP
PLAFEDTSSD FELPPLSLLT SPAQIERHHL SDEALEENAR MLESVLDDYG VKGDIVSVRP
GPVVTMYELE PAPGLKASRV IGLADDIARS MSALSARVST VPGRTVIGIE LPNDKREKVV
LREILASRDF GDGTHALPLA LGKDIGGDSM VANLAKMPHL LIAGTTGSGK SVAINTMILS
LLYKLTPEEC RLIMIDPKML ELSVYDGIPH LLSPVVTDPK KAVVALKWVV GEMEDRYRKM
SKMGVRNIAG YNGRVKEALD KGEMFSRTVQ TGFDDDTGEP VFETEEFAPE ALPYIVVIVD
EMADLMMVAG KEIEACIQRL AQMARASGIH LIMATQRPSV DVITGTIKAN FPTRISFQVT
SKVDSRTILG EMGAEQLLGM GDMLYMAGGA KITRCHGPFV SDEEVEEVVN HLKQFGPPEY
IGNVLDGPDD EKADNIDAVL GLSTGGNTDT EDALYDTAVQ IVIKDRKCST SYIQRKLAIG
YNKAARLVEQ MEEEGLVSPA NHVGKREILV PEQ
//
