ID Q1LMZ7_CUPMC Unreviewed; 1123 AA.
AC Q1LMZ7;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=DNA translocase ftsK, DNA segregation ATPase {ECO:0000313|EMBL:ABF08479.1};
GN Name=ftsK {ECO:0000313|EMBL:ABF08479.1};
GN OrderedLocusNames=Rmet_1596 {ECO:0000313|EMBL:ABF08479.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF08479.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CP000352; ABF08479.1; -; Genomic_DNA.
DR RefSeq; WP_011516326.1; NC_007973.1.
DR AlphaFoldDB; Q1LMZ7; -.
DR STRING; 266264.Rmet_1596; -.
DR KEGG; rme:Rmet_1596; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_14_1_4; -.
DR Proteomes; UP000002429; Chromosome.
DR GO; GO:0016020; C: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 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; 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; 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 68..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 769..978
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 116..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..264
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 531..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 786..793
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1123 AA; 117232 MW; 062C44556248D84D CRC64;
MGLGWFGLST LWLLPLVWQT VGRVLAGERR LLGRGSLRVL LGTVLVLGAS ATLESLTGGE
GETAGGAVGH ALAGVVSGML GWTGALLMML AVLGLTAPMV FGETWRSLFL LRKPRVESDE
DRGDTRTKSR ADSRFESRGS ARTTDSRHDA RSEPRGDFRS DSAAPQASPR DSVERWETTS
LPAQSAGGWQ ATQTRQKGIE AVSARRQPAW QPPPRTRESP PQPGEIWLHH AEAPGAVKPV
TPKPAPSSAQ KPSSTPPTPR AANPVPTAAR PAAAAPVQAK AEATVAPKPA APRATVVSSP
FRNPQLGLRS AITTLPEPAV ATTVAASAAT VAPAATAEVV EQAIDIAAVA AVATVADDLA
VERQDAPAAL ETSAALETSA VDGQSEASGE MPESSVTMDA IRDEALALLA ELQALAGRHV
QPSVAVEPSP VAEAVAEAAP MEAEALPAPI AESVLADVPD VPAEQGDADD MAIQLAVAAS
MAEAEIAQAE AIDEAPAEAE AEAATATAEQ ETTEAILAEA VPASDKASRP VVDAGDPESD
ESRIELQAEA EEAGEGEDQA DDSQTDDPSA VVDANTFVQP TPKPRIVLPA VVGRTVALGA
QAPATVAPVM AAPVPPSPPA APPAPPAPRI VDYRLPGASL LEAADENAEQ VSEERLEQTG
ELIAQRLAEF KVPVSVVGAS AGPVITRFEV DPAMGVRGAQ VVGLMKDLAR ALGVTSIRVV
ETIPGKTCMG LELPNAKRQM IRLSEIVNGG AFQAHASKLV LAMGKDITGN PVVTDLARAP
HLLVAGTTGS GKSVAVNAMI LSMLYKATPE DVRLIMIDPK MLELSVYEGI PHLLAPVVTD
MKQAAHALNW CVGEMEKRYR LMSALGVRNL AGYNQKIRVA EAAGEKVPNP FSLTPDAPEP
LSTLPLIVVV IDELADLMMV AGKKIEELIA RLAQKARAAG IHLILATQRP SVDVITGLIK
ANIPTRVAFQ VSSKIDSRTI LDQMGAESLL GQGDMLFLPP GTGYPQRVHG AFVADEEVHR
VVEHWKQFGE PDYDEAILAG DAPEGAADLF GDSGGDGESD PLYDEAAQFV LTSRRASISA
VQRQLRIGYN RAARLIEQME AAGLVSPMGR NGTREVLAPG PSD
//
