ID S5YQ53_PARAH Unreviewed; 940 AA.
AC S5YQ53;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=JCM7686_0307 {ECO:0000313|EMBL:AGT07416.1};
OS Paracoccus aminophilus JCM 7686.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=1367847 {ECO:0000313|EMBL:AGT07416.1, ECO:0000313|Proteomes:UP000015480};
RN [1] {ECO:0000313|EMBL:AGT07416.1, ECO:0000313|Proteomes:UP000015480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 7686 {ECO:0000313|EMBL:AGT07416.1};
RX PubMed=24517536; DOI=10.1186/1471-2164-15-124;
RA Dziewit L., Czarnecki J., Wibberg D., Radlinska M., Mrozek P., Szymczak M.,
RA Schluter A., Puhler A., Bartosik D.;
RT "Architecture and functions of a multipartite genome of the methylotrophic
RT bacterium Paracoccus aminophilus JCM 7686, containing primary and secondary
RT chromids.";
RL BMC Genomics 15:124-124(2014).
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; CP006650; AGT07416.1; -; Genomic_DNA.
DR RefSeq; WP_020949056.1; NC_022041.1.
DR AlphaFoldDB; S5YQ53; -.
DR STRING; 1367847.JCM7686_0307; -.
DR KEGG; pami:JCM7686_0307; -.
DR PATRIC; fig|1367847.3.peg.245; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_6_0_5; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000015480; Chromosome.
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:AGT07416.1};
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:UP000015480};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..185
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 206..224
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 576..795
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 323..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..390
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 593..600
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 940 AA; 101659 MW; B3B76F60DD84410E CRC64;
MASWQAKHRD PLFDQSTQAA LERRGKELLG AGLVVLGVLI AMMLISYTPD DPSIMSATDQ
PAANLLGRPG AYISSALFMI AGFGSYMLPL GAMVWGLRLV LHRGEDRIMR GIFLPLAMVL
VSIYATSLTP PPDWRQSFGL GGHLGDMLMG AMLSIMPMKA AIAIKILAFA VAIGAVAFST
FVFGFSKKEV ARFALFLRDG LRTARILLLK LLAGGAVLST HAAGEIRSRS AARRERTARA
GSAAIADEFA APDAPRAGFM SRLRRNGPAL PQDDLPPAEL YDREGNWADT EAPSNAEISA
RITDAIRSRN EKPSMMATVA ARLSGKGETP PRHEPPISTE LALDDDGLGD ETGHARPNAE
AFNRDFGTDL DGNFDGDLNG DLDGDDLDTD FGITAADRPA PQGEPSRRIV PPAPPVQPSR
QAMAEAQPRA SFEDTSRPHY EHPPLALLEA PATVERHQLS EEALTENARM LEAVLDDYGV
KGQITEVRPG PVVTLYELEP APGLKASRVI GLADDIARSM SALSARVSTV PGRTVIGIEL
PNARREKVVL REILASRAYG DGTFPLPLAL GKDIGGGPVV ANLAKMPHLL IAGTTGSGKS
VAINTMILSL LYKLTPEECR LIMIDPKMLE LSVYDGIPHL LSPVVTDPKK AVVALKWVVG
EMEERYRKMS KMGVRNIEGY NGRVREALSK NELFKRTVQT GFDEDTGEPV FETEEFKPET
FPYIVVIVDE MADLMMVAGK EIEACIQRLA QMARASGIHL IMATQRPSVD VITGTIKANF
PTRISFQVTS KIDSRTILGE QGAEQLLGQG DMLYMAGGSK ITRVHGPFVS DEEVEEIVRH
LKSFGPPTYM SGVVEGPDDE RADNIDMVLG LSTGEGGDAE LYDMAVAIVA KDRKCSTSYI
QRKLAIGYNK AARLVEQMEE QGVVSSANHV GKREVLIPEV
//
