ID B1ZGT6_METPB Unreviewed; 1136 AA.
AC B1ZGT6;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN OrderedLocusNames=Mpop_4516 {ECO:0000313|EMBL:ACB82614.1};
OS Methylorubrum populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
OS (Methylobacterium populi).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=441620 {ECO:0000313|EMBL:ACB82614.1, ECO:0000313|Proteomes:UP000007136};
RN [1] {ECO:0000313|EMBL:ACB82614.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJ001 {ECO:0000313|EMBL:ACB82614.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium populi BJ001.";
RL Submitted (APR-2008) 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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CP001029; ACB82614.1; -; Genomic_DNA.
DR AlphaFoldDB; B1ZGT6; -.
DR STRING; 441620.Mpop_4516; -.
DR KEGG; mpo:Mpop_4516; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_1_0_5; -.
DR Proteomes; UP000007136; Chromosome.
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: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; 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}; Cell cycle {ECO:0000313|EMBL:ACB82614.1};
KW Cell division {ECO:0000313|EMBL:ACB82614.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 734..953
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 9..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1040
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 237..287
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 14..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1019..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 751..758
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1136 AA; 120122 MW; 0AB9D16F7BE6428F CRC64;
MFRVISQIMR ASGRPPHSHR DPSRPSRGGD RLDRSIGGIA HRLMSLRSNL ARRIAGAPPA
PPRALPHALP HPALPHPGAD GFDAGTVPSW LVPPGTMLGR APAGQEPWPS KPWVSATEEG
LFEMPAPVHP GQHGAAQGLV HDGQPDMPFE SRIDPRASGP GVLVRTPRRP AAIAPETGTV
AHALPVSQPA PGGSYGVPQA PLPEAVRFTR TPDTVLMERR RQALEAEREA QARAQALLDA
QAAAEAAALE AQRAREAAEH EAAERAAQLA AEEAEAARLR AEQAVSEVPS WRRPFVPPPG
VSFFRTPDRR PKPVVPMQGS GQGAGQGTGP GAGQGGTQGA GAVPQPMPEP VIEAPRIEAA
APVAAEAESA TAFASLYAPF IPPVPAEPSD WSDVPDWSAL HGWFGPAEAM VEVAEPVAPP
ALRPVLNAMA ARAAIRSARS ALAEAAPILP VLPHAVAPAP AAAAAPVAVQ PAPTPIAMAP
QIPSPAPQAA PLTIAARPVL LRTKPGSETE EPAAEVVPSF VTEAFEESAQ EAAPEAAPES
APEIAPETAY AFEEGAAESV AAVEPAPENR PRAILPERPM LIPAGRHLEA SFVGNADYEL
PSLELLAEPP VGDGEEVDAD ELEQNALNLQ QTVQDFGVRG DILAVRPGPV VTLYELEPAP
GTKSSRVIGL SDDIARSMSA VSARVAVVPG RNVIGIELPN PVRETVYLRE LLASVDFVET
KHKLALCLGK NIGGEPIIAD LARMPHLLVA GTTGSGKSVA INTMILSLLY RLKPEECRLI
MVDPKMLELS VYDGIPHLLS PVVIDPKKAV IALKWAVREM EERYKKMSKI SVRNIDGYNA
RMKEARERGE IITRTVQTGF DRTTGEAVFE EQEMDLSALP YIVIVVDEMA DLMMVAGKDI
EGAIQRLAQM ARAAGIHLIM ATQRPSVDVI TGTIKANFPT RISFQVTSKI DSRTILGEMG
AEQLLGQGDM LFMAGGGRTT RVHGPFCSDS EVETVVAHLK AQGRPSYLEA VTADDGSSDQ
PEKPAKGSRA AAKAEKDDFA EAEEADAPVF DIGAFAATAG AEGGELYEQA IAVVLRDRKA
STSYIQRRLQ IGYNRAASIM ERMEIEGIVG PANHAGKREI LVEGLAGAPS GGYDDE
//
