ID A0A126RU69_9SPHN Unreviewed; 774 AA.
AC A0A126RU69;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=K426_20980 {ECO:0000313|EMBL:AMK25125.1};
OS Sphingobium sp. TKS.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1315974 {ECO:0000313|EMBL:AMK25125.1, ECO:0000313|Proteomes:UP000060779};
RN [1] {ECO:0000313|Proteomes:UP000060779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKS {ECO:0000313|Proteomes:UP000060779};
RA Tabata M.;
RT "Whole genome sequence of gamma-HCH degrading bacterium Sphingobium sp.
RT TKS.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AMK25125.1, ECO:0000313|Proteomes:UP000060779}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TKS {ECO:0000313|EMBL:AMK25125.1,
RC ECO:0000313|Proteomes:UP000060779};
RX PubMed=27056231;
RA Tabata M., Ohhata S., Kawasumi T., Nikawadori Y., Kishida K., Sato T.,
RA Ohtsubo Y., Tsuda M., Nagata Y.;
RT "Complete Genome Sequence of a gamma-Hexachlorocyclohexane Degrader,
RT Sphingobium sp. Strain TKS, Isolated from a gamma-Hexachlorocyclohexane-
RT Degrading Microbial Community.";
RL Genome Announc. 4:0-0(2016).
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; CP005083; AMK25125.1; -; Genomic_DNA.
DR RefSeq; WP_066561159.1; NZ_CP005083.1.
DR AlphaFoldDB; A0A126RU69; -.
DR STRING; 1315974.K426_20980; -.
DR KEGG; spht:K426_20980; -.
DR PATRIC; fig|1315974.3.peg.4408; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000060779; Chromosome 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000060779};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 135..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 409..628
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 240..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 753..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 426..433
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 774 AA; 84097 MW; 5915779086D05AA6 CRC64;
MAVSRGAKRT PEWREMLKRS LIRSGALIGS IALILATLFL ALALLSYQPS DPSMNTVAGD
HVQNIMQAPG AWIADFLLWL FGVPVALVLP LMAITARRLW GDQDMSGWKA QFGKCFAGIV
LLGIALALFQ TNPLVGLPAG WGGIIALVTA RGVLSLTAQA PVAQGWITGI LIVLTLIAGA
ILWYRSLALE KPIIALRRPS LPRLSLPKPA FALPGGGAVA DPFDDEDEVV ERIAAPRKTV
TNEPKPPINI QTPKPAPVQR PMAPVSQDDL FGNSSLPSPD LLNPIPASQG AKIDKAALER
NARLLESVLD DFHVKGNIVE VRPGPVVTMY ELEPAPGIKA SRVIALADDI ARNMSALSAR
VATIPGRTVI GIELPNANRE GVSFRELITS EQFMQEATLP IILGKNISGE PIIADLAPMP
HLLIAGTTGS GKSVGLNAMI LSLLYRMTPD QLRLIMIDPK MLELSTYDDI PHLLSPVVTE
PSKAIRALKW AVEQMEDRYR MMASISVRNL ANYNEKVRAA KAKGKPLGRR VQTGYDPENG
KPIYEEEQLD FQPLPQIVVV VDELADLMMT AGKEVEFLIQ RLAQKARAAG IHLILATQRP
SVDVITGVIK ANLPTRISFF VTSKIDSRTI LGEQGAEQLL GKGDMLYMHG GKGLMRVHGP
FVSDDEVRVV ADHWRAQGQP DYIAAVTEEP EEGSFALDGV DLGDDSPDAQ LFRKACQLVF
ENQKASTSWL QRQLRIGYNS AARLIEQMEE QGLVGPPNHV GRREVLRDEG GNPL
//