ID A0A0L6CVR5_9RHOB Unreviewed; 964 AA.
AC A0A0L6CVR5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN Name=ftsK {ECO:0000313|EMBL:KNX41836.1};
GN ORFNames=ROTO_15610 {ECO:0000313|EMBL:KNX41836.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX41836.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-2015) 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:KNX41836.1}.
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DR EMBL; LGVV01000016; KNX41836.1; -; Genomic_DNA.
DR RefSeq; WP_050662472.1; NZ_LGVV01000016.1.
DR AlphaFoldDB; A0A0L6CVR5; -.
DR STRING; 74031.SAMN04488077_109109; -.
DR PATRIC; fig|74031.6.peg.1594; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000037046; 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:UP000037046};
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..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 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 598..817
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 615..622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 964 AA; 103988 MW; 3FDD7D34338947CB CRC64;
MAYQTRGRDP LLDSTTAEAI EKRGKELLGL VLVVIALMTA AMVASYSPDD PSWVSATDEP
VQNWMGRVGA AIASPLFMII GWGAWGLAIV LGAWGVRFAL HLGEDRATGR LIFAPIWLAV
LSLYAATLAP GEAWAATHSF GLGGLFGDTI LGTFLGVLPV AASLGLKLMS VVMGLCVLVF
GAFVLGFTRF ELGRIARFLL VGVIVSYSGL MRLLGHGAGG MAQAGQAVQA RIAERRARRA
EAVVYEEDAP VAEAPRVRRA EPVLGAAPQM AAAEKPGGLL ARMPMLMRRP DPMPEPELVE
SESYHGEAEQ PADDRIKARI SDVIRARVRQ NPAVQAASVA PLTKGRGRGP DPLILNTAPR
EGLPPEPPLT ARHAETVAPA PVEQDPVIER DDLYAPESEM DDEMAAYLAE SAPQPQAAPR
IPVPEPRKVV QHTPRKAPQP STRAIAEAQP ALQFEEPALP EYELPPLSLL SDPTRIERHH
LSDEALEENA RMLENVLDDY GVKGEIVSVR PGPVVTMYEL EPAPGLKASR VIGLADDIAR
SMSALSARVS TVPGRSVIGI ELPNDNREMV GFREILSSRA YGDGNQRLPL ALGKDIGGDP
MVANLAKMPH LLIAGTTGSG KSVAINTMIL SLLYKLTPDE CRLIMIDPKM LELSVYDGIP
HLLSPVVTDP KKAVVALKWV VAEMEDRYRK MSKMGVRNID GYNGRVEEAL KKGELFSRTV
QTGFDDDTGE PVFETEEFAP EKMPYIVVIV DEMADLMMVA GKEIEACIQR LAQMARASGI
HLIMATQRPS VDVITGTIKA NFPTRISFQV TSKIDSRTIL GEMGAEQLLG MGDMLYMAGG
GKITRCHGPF VSDEEVEEVV SHLKAYGPPE YVGSVLQGPD EDKADSIDAV LGLSTGGNTD
GEDALYDQAV AIVIKDRKCS TSYIQRKLAI GYNKAARLVE QMEDEGVVSA ANHVGKREVL
VPEQ
//
