ID FTSK_RHILO Reviewed; 887 AA.
AC Q98EH3;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=mll4243;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Located at the septum.
CC {ECO:0000250}.
CC -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for the
CC localization to the septal ring and is required for cell division,
CC followed by a linker domain, and a C-terminal domain, which forms the
CC translocation motor involved in chromosome segregation. The C-terminal
CC domain can be further subdivided into alpha, beta and gamma subdomains.
CC The alpha and beta subdomains multimerise to produce a hexameric ring,
CC contain the nucleotide binding motif and form the DNA pump. The gamma
CC subdomain is a regulatory subdomain that controls translocation of DNA
CC by recognition of KOPS motifs and interacts with XerD recombinase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; BA000012; BAB50946.1; -; Genomic_DNA.
DR RefSeq; WP_010912288.1; NC_002678.2.
DR AlphaFoldDB; Q98EH3; -.
DR SMR; Q98EH3; -.
DR KEGG; mlo:mll4243; -.
DR PATRIC; fig|266835.9.peg.3348; -.
DR eggNOG; COG1674; Bacteria.
DR eggNOG; COG2261; Bacteria.
DR HOGENOM; CLU_001981_6_1_5; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0007059; P:chromosome segregation; 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; Cell cycle; Cell division; Cell inner membrane; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..887
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098284"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..133
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..887
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 515..734
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 794..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 535..540
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 887 AA; 96130 MW; 9AC9AA38D13CA863 CRC64;
MRSGASAPLA MTDTGHGIQA FARRQVGRLV GAGMFLAVAF GVASLATWNV ADPSFSHATN
NTVTNAMGYA GAVFSDLAMQ FFGLAAVAAL VPAVIWGYLL FSARGVDRLP KRGLFWFGFA
LLAAAIAGCI VPPKTWPLPT GLGGVFGDMV LKIPGVLIGG YPTGLIASVL AVLLAGPTLW
LFAFGSALIG RKNGFAVMEE PAAADPREDD LLFDNEEDEG DEGILALGAI THWWLSLRAW
MHRRAVRRRQ ERDEYEPEME PRASAWRRAA ERVESAEFAE QRMSPGGRAR VEPEFFAAMV
NDRSVSVDPD DDDIFDRDDE DMDFDDEPVA QRRAAPAAKV QQFRSDAATR VEAPAPRPAP
GARVQREAQT SLIGSDKFEM PSLHFLSEPK NVARDPSLSK DALEQNARLL EGVLEDFGVK
GEIIAVRPGP VVTLYELEPA PGIKSSRVIG LSDDIARSMS AIACRVAVVP GRNAIGIELP
NAKRETVYLR EIMASRDFET TKAKLALALG KTINGEAVIV DIAKMPHVLV AGTTGSGKSV
AINTMILSLL YRLTPQECRL IMIDPKMLEL SVYDGIPHLL TPVVTDPKKA VVALKWTVRE
MEDRYRKMSK VGVRNIDGFN ARVQLAEKKG EKISRTVQTG FDRQTGEAIY ETEDLDLEPM
PYIVVIIDEM ADLMMVAGKD IEGAVQRLAQ MARAAGIHVI MATQRPSVDV ITGTIKANFP
TRISFQVTSK IDSRTILGEQ GAEQLLGMGD MLYMAGGGRI QRVHGPFVSD DEVEKIVGHL
KLQGVPEYLD AITEDDDEDD DEPSGKGAGS GGGGGGNFED SDDPYDQAVA VVLRDGKAST
SYIQRRLGIG YNRAASIIEK MEKEGIVGPA NHAGKREILV PTEDDKF
//
