ID FTSK_RHIME Reviewed; 881 AA.
AC Q92L89;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=R03191; ORFNames=SMc03808;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; AL591688; CAC47770.1; -; Genomic_DNA.
DR RefSeq; NP_387297.1; NC_003047.1.
DR RefSeq; WP_010970484.1; NC_003047.1.
DR AlphaFoldDB; Q92L89; -.
DR SMR; Q92L89; -.
DR EnsemblBacteria; CAC47770; CAC47770; SMc03808.
DR GeneID; 61604650; -.
DR KEGG; sme:SMc03808; -.
DR PATRIC; fig|266834.11.peg.4741; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_5; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000001976; 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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..881
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098285"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 81..101
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..881
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 514..733
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 194..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 793..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534..539
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 881 AA; 95549 MW; 28E890501D72585F CRC64;
MSRSNTATLD SRSNRFVLTH FVWRQIASLA GFVLVGALAL AIAALSTWNV ADPSFSYATS
NEPTNLLGYG GAVFADIFMQ FFGLASVVAL LPAVAWALVL IRGTHFDKVL KRLGLWFAGS
VLASAALSCV PAPITWPLPN GLGGVFGDMI LRFPALFTGT FPTGTFATVL ACLFTAPAAW
CLVYSAGLIG VSEDEEAEPA PEPAPSKART IRDELEEEDE EGPLTVLMGS LAHMRYTAQA
RLRRAFGMGA KPAKRQYDEP YDFNNDEFGT LNEPVRPKAQ AGRIEPSLDR SERRIVTPPP
IMGDEDDPPF DIDERRPAGI LPDDDEDDVA ADWAPRPAPP KPALAMAGSR VAPPRPKAGQ
RVEREAQRSF VDEDGDFTLP PIHFLAEPKN VARDASLSAD ALEQNARMLE GVLEDFGVKG
EIIHVRPGPV VTLYELEPAP GIKSSRVIGL ADDIARSMSA IAARVAVVPG RNAIGIELPN
QRREMVYLRE LIGSRDFETT KTKLAMALGK TIGGESVVAD LAKMPHLLVA GTTGSGKSVA
INTMILSLLY RLRPDQCRLI MIDPKMLELS VYDGIPHLLS PVVTDPKKAV VALKWTVREM
EERYKKMSKI GVRNIDGFNS RVEQALAKGE AITRTVQTGF DRQTGEAVYE TEEFDLSPMP
YIVVIIDEMA DLMMVAGKDI EGAVQRLAQM ARAAGIHVIM ATQRPSVDVI TGTIKANFPT
RISFQVTSKI DSRTILGEQG AEQLLGMGDM LYMAGGGRIQ RVHGPFVSDT EVEEVVAYLK
TQGVPQYLDA ITEDDEDEND GGGPAGTSNL ADSEDPYDQA VAIVLRDGKA STSYVQRRLG
IGYNRAASLI ERMEQEGIIS PANHAGKREI LVPTEAEITG R
//
