FTSK_PSEAE
ID FTSK_PSEAE Reviewed; 811 AA.
AC Q9I0M3;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=PA2615;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 247-811 IN COMPLEX WITH ADP,
RP FUNCTION AS A TRANSLOCASE, AND SUBUNIT.
RX PubMed=16916635; DOI=10.1016/j.molcel.2006.06.019;
RA Massey T.H., Mercogliano C.P., Yates J., Sherratt D.J., Lowe J.;
RT "Double-stranded DNA translocation: structure and mechanism of hexameric
RT FtsK.";
RL Mol. Cell 23:457-469(2006).
RN [3]
RP STRUCTURE BY NMR OF 739-811, DNA-BINDING, AND DOMAIN.
RX PubMed=17057717; DOI=10.1038/nsmb1158;
RA Sivanathan V., Allen M.D., de Bekker C., Baker R., Arciszewska L.K.,
RA Freund S.M., Bycroft M., Lowe J., Sherratt D.J.;
RT "The FtsK gamma domain directs oriented DNA translocation by interacting
RT with KOPS.";
RL Nat. Struct. Mol. Biol. 13:965-972(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 739-811, FUNCTION, SUBUNIT, AND
RP DNA-BINDING.
RX PubMed=18722176; DOI=10.1016/j.molcel.2008.05.027;
RA Lowe J., Ellonen A., Allen M.D., Atkinson C., Sherratt D.J., Grainge I.;
RT "Molecular mechanism of sequence-directed DNA loading and translocation by
RT FtsK.";
RL Mol. Cell 31:498-509(2008).
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 (Probable).
CC {ECO:0000305|PubMed:16916635, ECO:0000305|PubMed:18722176}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000269|PubMed:16916635, ECO:0000269|PubMed:18722176}.
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
CC (Probable). {ECO:0000305|PubMed:17057717}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG06003.1; -; Genomic_DNA.
DR PIR; E83318; E83318.
DR RefSeq; NP_251305.1; NC_002516.2.
DR RefSeq; WP_010895627.1; NZ_QZGE01000008.1.
DR PDB; 2IUT; X-ray; 2.25 A; A/B=247-811.
DR PDB; 2IUU; X-ray; 2.90 A; A/B/C/D/E/F=247-728.
DR PDB; 2J5O; NMR; -; A=742-811.
DR PDB; 2VE8; X-ray; 1.40 A; A/B/C/D/E/F/G/H=739-811.
DR PDB; 2VE9; X-ray; 1.90 A; A/B/C/D/E/F=739-811.
DR PDB; 6T8B; EM; 3.65 A; A/B/C/D/E/F=247-728.
DR PDB; 6T8G; EM; 4.34 A; A/B/C/D/E/F=247-728.
DR PDB; 6T8O; EM; 3.99 A; A/B/C/D/E/F=247-728.
DR PDBsum; 2IUT; -.
DR PDBsum; 2IUU; -.
DR PDBsum; 2J5O; -.
DR PDBsum; 2VE8; -.
DR PDBsum; 2VE9; -.
DR PDBsum; 6T8B; -.
DR PDBsum; 6T8G; -.
DR PDBsum; 6T8O; -.
DR AlphaFoldDB; Q9I0M3; -.
DR SMR; Q9I0M3; -.
DR STRING; 287.DR97_5347; -.
DR PaxDb; Q9I0M3; -.
DR PRIDE; Q9I0M3; -.
DR EnsemblBacteria; AAG06003; AAG06003; PA2615.
DR GeneID; 882321; -.
DR KEGG; pae:PA2615; -.
DR PATRIC; fig|208964.12.peg.2736; -.
DR PseudoCAP; PA2615; -.
DR HOGENOM; CLU_001981_9_7_6; -.
DR InParanoid; Q9I0M3; -.
DR OMA; YKAEARD; -.
DR PhylomeDB; Q9I0M3; -.
DR BioCyc; PAER208964:G1FZ6-2655-MON; -.
DR EvolutionaryTrace; Q9I0M3; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0071236; P:cellular response to antibiotic; IMP:PseudoCAP.
DR GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 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; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Chromosome partition; DNA-binding; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..811
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098278"
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 73..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..138
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..811
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 449..661
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 269..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..474
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 675
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT BINDING 693..694
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 333..349
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 356..361
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 385..392
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 398..401
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 423..427
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 438..446
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 456..458
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 462..465
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 472..484
FT /evidence="ECO:0007829|PDB:2IUT"
FT TURN 489..491
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 502..505
FT /evidence="ECO:0007829|PDB:2IUT"
FT TURN 506..509
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 521..545
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 550..562
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 575..578
FT /evidence="ECO:0007829|PDB:2IUU"
FT STRAND 589..595
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 600..603
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 606..618
FT /evidence="ECO:0007829|PDB:2IUT"
FT TURN 620..623
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 624..631
FT /evidence="ECO:0007829|PDB:2IUT"
FT TURN 635..637
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 640..644
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 648..652
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 657..664
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 665..667
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 669..671
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 677..681
FT /evidence="ECO:0007829|PDB:2IUT"
FT STRAND 683..686
FT /evidence="ECO:0007829|PDB:2IUU"
FT STRAND 689..693
FT /evidence="ECO:0007829|PDB:2IUT"
FT HELIX 698..709
FT /evidence="ECO:0007829|PDB:2IUT"
FT TURN 718..721
FT /evidence="ECO:0007829|PDB:2IUU"
FT STRAND 742..746
FT /evidence="ECO:0007829|PDB:2J5O"
FT HELIX 750..760
FT /evidence="ECO:0007829|PDB:2VE8"
FT HELIX 765..772
FT /evidence="ECO:0007829|PDB:2VE8"
FT HELIX 776..788
FT /evidence="ECO:0007829|PDB:2VE8"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:2J5O"
SQ SEQUENCE 811 AA; 88894 MW; 3174CA63E8190405 CRC64;
MRRKNSDLKD STTASHAAAW RQQLHSRLKE GVLIALGALC LYLWMALLTY DSADPSWSHS
SQVDQVQNAA GRLGAVSADI LFMTLGYFAY LFPLLLGIKT WQVFRRRNLP WEWNTWLFSW
RLVGLIFLIL AGSALAYIHF HASGHMPASA SAGGAIGQSL GRVAVDALNV QGSTLVFFAL
FLFGLTVFAD LSWFKVMDVT GKITLDFFEL IQNAFNRWMG ARAERKQLVA QLREVDERVA
EVVAPSVPDR REQSKAKERL LEREEALAKH MSEREKRPPP KIDPPPSPKA PEPSKRVLKE
KQAPLFVDTA VEGTLPPLSL LDPAEVKQKS YSPESLEAMS RLLEIKLKEF GVEVSVDSVH
PGPVITRFEI QPAAGVKVSR ISNLAKDLAR SLAVISVRVV EVIPGKTTVG IEIPNEDRQM
VRFSEVLSSP EYDEHKSTVP LALGHDIGGR PIITDLAKMP HLLVAGTTGS GKSVGVNAML
LSILFKSTPS EARLIMIDPK MLELSIYEGI PHLLCPVVTD MKEAANALRW SVAEMERRYR
LMAAMGVRNL AGFNRKVKDA EEAGTPLTDP LFRRESPDDE PPQLSTLPTI VVVVDEFADM
MMIVGKKVEE LIARIAQKAR AAGIHLILAT QRPSVDVITG LIKANIPTRI AFQVSSKIDS
RTILDQGGAE QLLGHGDMLY LPPGTGLPIR VHGAFVSDDE VHRVVEAWKL RGAPDYIEDI
LAGVDEGGGG GGSFDGGDGS GEGSEDDPLY DEAVRFVTES RRASISAVQR KLKIGYNRAA
RMIEAMEMAG VVTPMNTNGS REVIAPAPVR D
