ID B1LX19_METRJ Unreviewed; 1135 AA.
AC B1LX19;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN OrderedLocusNames=Mrad2831_3749 {ECO:0000313|EMBL:ACB25724.1};
OS Methylobacterium radiotolerans (strain ATCC 27329 / DSM 1819 / JCM 2831 /
OS NBRC 15690 / NCIMB 10815 / 0-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426355 {ECO:0000313|EMBL:ACB25724.1, ECO:0000313|Proteomes:UP000006589};
RN [1] {ECO:0000313|EMBL:ACB25724.1, ECO:0000313|Proteomes:UP000006589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27329 / DSM 1819 / JCM 2831 / NBRC 15690 / NCIMB 10815 /
RC 0-1 {ECO:0000313|Proteomes:UP000006589};
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., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium radiotolerans JCM
RT 2831.";
RL Submitted (MAR-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; CP001001; ACB25724.1; -; Genomic_DNA.
DR AlphaFoldDB; B1LX19; -.
DR STRING; 426355.Mrad2831_3749; -.
DR KEGG; mrd:Mrad2831_3749; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_1_0_5; -.
DR Proteomes; UP000006589; 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:ACB25724.1};
KW Cell division {ECO:0000313|EMBL:ACB25724.1};
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 731..950
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 47..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1048
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 189..241
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 748..755
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1135 AA; 120187 MW; 749673C3868BC082 CRC64;
MRASGRPPYS HRDPARPVRG GDRSGLSLGA LAHRLMALRA SLTRRLSGSP AGLPARPSYG
APGRRAEPSW LTPPGAMVGR EGSERAARAA APEPHWPAQV FDDRASLDVL DGPALESRID
RSASSPGVLV RQPRRPAAIA PDYAPAAAPA AGHVAGHVAA PVHASAPAAA PSAVRYTRTP
DSVLQERRQR ALEAERVALE RARAEAQAAA LALETERAAR EEAERERIER ARVAAEEAER
AAPVPALPEA SAPDAEPVPL WRQPFVAPPG VRFFRTPDRR PVRPAVELTA STAAIAPVAA
APVAAALVET VAEAPARDWS DLPDWSEVQP WFDGGDWSSV DAWSALEAPP AEVAPTPAAV
AAPAASDERF VSMPLDVSHL RSLPPRPVYV LDRLVRFDQP PRPADGQDNG TEAGPRMEEA
ATIRSAFLPP VAPTAASGLS LVFGPGSAAA EPPATPVSEA PRRAPALSAM AARAAIRAAG
QPSVVPPAPP AQPEPAPAPV SAAPVAARAE AERVVIPMTP RPVLLRGKLA PQPEPVEANV
AAETEAEPAA AAVEAVEVPA LPAPAPASVP LVAPRAHLIP AGRHLEIAPI ENADYELPSL
ELLALPAPGG SEEVDADVLE QNALNLQQTV QDFGVRGDIL AVRPGPVVTL YELEPAPGTK
SSRVIGLSDD IARSMSAVSA RVAVVPGRNV IGIELPNETR ETVYLRELLS SADFAESKHK
LALCLGKNIG GEPIIADLAR MPHLLVAGTT GSGKSVAINT MILSLLYRLK PEECRLIMVD
PKMLELSVYD GIPHLLSPVV IDPKKAVIAL KWAVREMEER YKKMAKIAVR NIDGYNARMK
EARDRGETIT RTIQTGFDRH TGEAVYEDEA MDLAPLPYIV IVVDEMADLM MVAGKDIEGA
IQRLAQMARA AGIHLIMATQ RPSVDVITGT IKANFPTRIS FQVTSKIDSR TILGEMGAEQ
LLGQGDMLFM AGGGRTTRVH GPFCSDSEVE SVVAHLKRQG RPSYLDAVTA DDTPEEPAKE
GGRSGRGSKA AAADKAERSD EPEEEAPVFD IGAFAAATGG ESDDLYKQAI EVVLRDQKAS
TSYIQRRLQI GYNRAASIME RMEIEGIVGP ANHAGKREIL VAGATHSSAG MYDDE
//
