FTSK_YERPE
ID FTSK_YERPE Reviewed; 1305 AA.
AC Q8ZGC7; Q0WH39;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=YPO1376, y2800, YP_1217;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
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; AL590842; CAL20028.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM86350.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61460.1; -; Genomic_DNA.
DR PIR; AB0168; AB0168.
DR RefSeq; WP_002211339.1; NZ_WUCL01000089.1.
DR RefSeq; YP_002346399.1; NC_003143.1.
DR AlphaFoldDB; Q8ZGC7; -.
DR SMR; Q8ZGC7; -.
DR STRING; 214092.YPO1376; -.
DR PaxDb; Q8ZGC7; -.
DR DNASU; 1147746; -.
DR EnsemblBacteria; AAM86350; AAM86350; y2800.
DR EnsemblBacteria; AAS61460; AAS61460; YP_1217.
DR GeneID; 57977172; -.
DR KEGG; ype:YPO1376; -.
DR KEGG; ypk:y2800; -.
DR KEGG; ypm:YP_1217; -.
DR PATRIC; fig|214092.21.peg.1699; -.
DR eggNOG; COG1674; Bacteria.
DR eggNOG; COG3107; Bacteria.
DR HOGENOM; CLU_001981_0_2_6; -.
DR OMA; DPFWKPG; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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: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 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..1305
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098323"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 188..1305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 949..1162
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 405..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 518..550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 578..602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1286..1305
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..550
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 969..974
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT CONFLICT 172
FT /note="V -> A (in Ref. 3; AAS61460)"
FT /evidence="ECO:0000305"
FT CONFLICT 289
FT /note="T -> A (in Ref. 3; AAS61460)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="T -> A (in Ref. 3; AAS61460)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1305 AA; 140682 MW; DD25C959541F1839 CRC64;
MSQEYTEDKE VTLKKLSNGR RLLEAVLIVV TILAAYLMVA LVSFNPSDPS WSQTAWHEPI
HNLGGSIGAW MADTLFSTFG VLAYAIPPIM VIFCWTAFRQ RDASEYLDYF ALSLRLIGTL
ALILTSCGLA ALNIDDLYYF ASGGVIGSLF SNAMLPWFNG VGATLTLLCI WVVGLTLFTG
WSWLVIAEKI GAAVLGSLTF ITNRSRREER YDDEDSYHDD DHADGRDITG QEKGVVSNKG
VVSNNAVVGA GVAASSALAH GDDDVLFSAP SVTDSIVEHG SVVATGTETT DTKATDTNDE
YDPLLSPLRA TDYSVQDATS SPIADVAVEP VLNHDAAAIY GTTPVMTNTA TPPLYSFELP
EESLPIQTHA APTERPEPKL GAWDMSPTPV SHSPFDFSAI QRPVGQLESR QPGSNQSGSH
QIHSAQSSHI SVGNTPYMNP GLDAQIDGLS TTSLTNKPVL ASGTVAAATA AAAFMPAFTA
TSDSSSQIKQ GIGPELPRPN PVRIPTRREL ASFGIKLPSQ RMAEQELRER DGDETQNPQM
AASSYGTEIT SDEDAALQQA ILRKAFADQQ SERYALSTLA EQSSITERSP AAEMPTTPSQ
VSDLEDEQAL QEAELRQAFA AQQQHRYGAT GDTDNAVDNI RSVDTSTAFT FSPIADLVDD
SPREPLFTLS PYVDETDVDE PVQLEGKEES LLQDYPEQVP TYQPPVQQAH LGQSAPTQPS
HTQSTYGQST YGQSTYGQST PAPVSQPVVT SASAISTSVT PTSIASLNTA PVSAAPVAPS
PQPPAFSQPT AAMDSLIHPF LMRNDQPLQK PTTPLPTLDL LSSPPAEEEP VDMFALEQTA
RLVEARLGDY RVKAEVVGIS PGPVITRFEL DLAPGVKASR ISNLSRDLAR SLSAIAVRVV
EVIPGKPYVG LELPNKHRQT VYLREVLDCA KFRENPSPLA IVLGKDIAGQ PVVADLAKMP
HLLVAGTTGS GKSVGVNAMI LSILYKATPD DVRFIMIDPK MLELSVYEGI PHLLTGVVTD
MKDAANALRW CVGEMERRYK LMSALGVRNL AGYNERVAQA EAMGRPIPDP FWKPSDSMDI
SPPMLVKLPY IVVMVDEFAD LMMTVGKKVE ELIARLAQKA RAAGIHLVLA TQRPSVDVIT
GLIKANIPTR IAFTVSSKID SRTILDQGGA ESLLGMGDML YMAPNSSIPV RVHGAFVRDQ
EVHAVVNDWK ARGRPQYIDS ILSGGEEGEG GGLGLDSDEE LDPLFDQAVN FVLEKRRASI
SGVQRQFRIG YNRAARIIEQ MEAQQIVSTP GHNGNREVLA PPPHE
