ID K2K6U8_9PROT Unreviewed; 813 AA.
AC K2K6U8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=P24_03301 {ECO:0000313|EMBL:EKE78554.1};
OS Oceanibaculum indicum P24.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Oceanibaculaceae; Oceanibaculum.
OX NCBI_TaxID=1207063 {ECO:0000313|EMBL:EKE78554.1, ECO:0000313|Proteomes:UP000006746};
RN [1] {ECO:0000313|EMBL:EKE78554.1, ECO:0000313|Proteomes:UP000006746}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P24 {ECO:0000313|EMBL:EKE78554.1,
RC ECO:0000313|Proteomes:UP000006746};
RX PubMed=23209207; DOI=10.1128/JB.01859-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of Oceanibaculum indicum Type Strain P24.";
RL J. Bacteriol. 194:6942-6942(2012).
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:EKE78554.1}.
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DR EMBL; AMRL01000002; EKE78554.1; -; Genomic_DNA.
DR RefSeq; WP_008943277.1; NZ_AMRL01000002.1.
DR AlphaFoldDB; K2K6U8; -.
DR STRING; 1207063.P24_03301; -.
DR PATRIC; fig|1207063.3.peg.670; -.
DR eggNOG; COG1674; Bacteria.
DR Proteomes; UP000006746; 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:UP000006746};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 450..669
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 245..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 813 AA; 86778 MW; EC74EE62B8BC7EAB CRC64;
MATTSNATTR TALFPPGFAA FLKRRAREAS GLALIALAVA LVLAMASYHP QDPSLNTANT
GPIRNWLGYP GALAGDLLLQ TLGLSGGLLA LVIAAWGYRI LARLGVARVV LRVALLPLGL
LLAAMALAVV TPPAGWPLVS GLGGFTGTLL LAKAGGLLPL LGASVELALV GLVAGLLSAL
LLLYTLGFSL REWWALMRRS ARMAWAGGAL TYRGAAASGR LGGRLGGAAA KAGYDLARKG
LRQEPSLKGN ALSRDRAAAE EDEAEDMPRA ARSPRLEMPR EPAAATPKEA RLEKRSPAKS
ASKQKSLDLA PSGDFELPEM ELLTPAPARR SGPQPEGLEA NARLLETVLS DFGVKGEIVK
IRPGPVVTLY ELEPAPGTKS SRVIGLSDDI ARSMSAVSVR VAVVPGRSVI GIELPNQNRE
TVFLRETFES DAYERSAAKL PLALGHDIGG VPVIADLARM PHLLVAGTTG SGKSVAVNAM
ILSLLYKLPP ERCRFIMIDP KMLELSIYDG IPHLLAPVVT DPSKAVVALK WTVREMENRY
RAMSKLGVRN IDGYNLRLAE ARKKGEVLKR RVQTGFDADT GKPVFEDETL DLEPLPYIVV
VVDEMADLML VAGKDIEAAI QRLAQMARAA GIHIIMATQR PSVDVITGTI KANFPTRISF
QVTSKIDSRT ILGEGGAETL LGQGDMLYMA GGGRLTRVHG PFVSDGEVED VVRHLKAQGV
PDYVESVTED DDLGGDIAGL SGGDSDGERD DLFDRAVELV AREGKCSTSF IQRYLQIGYN
RAARIVERME AEGMVSKANH VGKREVLLRD PDE
//
