ID A0A1X4IXX8_9RHOB Unreviewed; 975 AA.
AC A0A1X4IXX8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=BV911_09505 {ECO:0000313|EMBL:OSP55052.1};
OS Pseudoruegeria sp. SK021.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Pseudoruegeria.
OX NCBI_TaxID=1933035 {ECO:0000313|EMBL:OSP55052.1, ECO:0000313|Proteomes:UP000194129};
RN [1] {ECO:0000313|EMBL:OSP55052.1, ECO:0000313|Proteomes:UP000194129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK021 {ECO:0000313|EMBL:OSP55052.1,
RC ECO:0000313|Proteomes:UP000194129};
RA Pohlner M., Marshall I., Schreiber L., Cypionka H., Engelen B.;
RT "Draft genome sequence of Pseudoruegeria str. SK021, a representative of
RT the marine Rosebacter group, isolated from North Sea sediment.";
RL Submitted (JAN-2017) 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 -!- 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:OSP55052.1}.
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DR EMBL; MTBG01000012; OSP55052.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4IXX8; -.
DR STRING; 1933035.BV911_09505; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000194129; 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, ECO:0000313|EMBL:OSP55052.1};
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:UP000194129};
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..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 67..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 610..829
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 336..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 627..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 975 AA; 105536 MW; B93A693F18661B36 CRC64;
MAYQTRRRDP LFDQATQVAL EKRARELMGV ALFVGATLLA LALASYSPTD PSFLGTSSEA
PQNWLGYFGA YLAAPLYVIL GAGSWALVAV GMVWGVRFAF HLGEDRAFGR LIFVPVFVAV
AAVYAATYPP GAEWVHSFGM GGLFGDTALG VLLGILPLAP SFGLLLSAAA LAILMLAAGL
HALGFTRPEL AGMGRFLWFG TLFAFDGLIR KLGHGASRTR EQLVERVERR KELRAERRQF
DDEMLVDEDD GVMAPSYDRP AATLPPVPKL GGAARTISRD EPMLSARYAP EPLMFEAEDD
DYDDEVFEET TQPGPGGDQR VRAKITDAIR LRLRSDRARA AAASRNRREP VLSRHEPTAP
EITAEPASMF VRATPRPAAP AASRMPLPAA GAPAAFAASK AAAYDQTAFV DSDDDDDDYD
DYSAQEPAIS GDAARFHDPK PVVRHAVKRP AVAQQTGGAA QPSHQPTHTD DDGYETPPLS
LLADPSIVER LHLSDEALEE NARMLENVLD DYGVKGDIVS VRPGPVVTMY ELEPAPGLKA
SRVIGLADDI ARSMSALSAR VSTVPGRSVI GIELPNEKRE MVLLREILAA RDFGDSKMRL
PLALGKDIGG EAIVANLAKM PHLLIAGTTG SGKSVAINTM ILSLLYKLTP AECRLIMIDP
KMLELSVYDD IPHLLSPVVT DPKKAVVALK WVVAEMEDRY RKMSKMGVRN IEGYNGKVRA
TLDKGEMFSR TVQTGFDDET GDPVFETEEF APETLPYIVV IVDEMADLMM VAGKEIEACI
QRLAQMARAS GIHLIMATQR PSVDVITGTI KANFPTRISF QVTSKIDSRT ILGEQGAEQL
LGMGDMLYMA GGGRITRIHA PFVSDEEVEV VVNHLKSMGS PSYVGGVADG PDDDKSDDID
LILGLGGNTG GEDALYDQAV QIVIQDRKCS TSYIQRKLAI GYNKAARLVE QMEDNGLVSP
ANHVGKRDVL VPEQQ
//
