FTSK_ECOLI
ID FTSK_ECOLI Reviewed; 1329 AA.
AC P46889; P77450;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=b0890, JW0873;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT TOE44.
RC STRAIN=K12;
RX PubMed=7592387; DOI=10.1128/jb.177.21.6211-6222.1995;
RA Begg K.J., Dewar S.J., Donachie W.D.;
RT "A new Escherichia coli cell division gene, ftsK.";
RL J. Bacteriol. 177:6211-6222(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN CHROMOSOME SEGREGATION, AND DOMAIN.
RX PubMed=9829960; DOI=10.1128/jb.180.23.6424-6428.1998;
RA Yu X.C., Weihe E.K., Margolin W.;
RT "Role of the C terminus of FtsK in Escherichia coli chromosome
RT segregation.";
RL J. Bacteriol. 180:6424-6428(1998).
RN [6]
RP FUNCTION IN CELL DIVISION, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=9723913; DOI=10.1046/j.1365-2958.1998.00958.x;
RA Wang L., Lutkenhaus J.;
RT "FtsK is an essential cell division protein that is localized to the septum
RT and induced as part of the SOS response.";
RL Mol. Microbiol. 29:731-740(1998).
RN [7]
RP MUTAGENESIS OF GLU-58, AND TOPOLOGY.
RX PubMed=10922461; DOI=10.1016/s0014-5793(00)01820-2;
RA Dorazi R., Dewar S.J.;
RT "Membrane topology of the N-terminus of the Escherichia coli FtsK division
RT protein.";
RL FEBS Lett. 478:13-18(2000).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11703663; DOI=10.1046/j.1365-2958.2001.02640.x;
RA Chen J.C., Beckwith J.;
RT "FtsQ, FtsL and FtsI require FtsK, but not FtsN, for co-localization with
RT FtsZ during Escherichia coli cell division.";
RL Mol. Microbiol. 42:395-413(2001).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=11948172; DOI=10.1128/jb.184.9.2552-2556.2002;
RA Hale C.A., de Boer P.A.J.;
RT "ZipA is required for recruitment of FtsK, FtsQ, FtsL, and FtsN to the
RT septal ring in Escherichia coli.";
RL J. Bacteriol. 184:2552-2556(2002).
RN [10]
RP FUNCTION, HEXAMERIZATION, AND FUNCTION IN REGULATION OF XERC AND XERD.
RX PubMed=11832210; DOI=10.1016/s0092-8674(02)00624-4;
RA Aussel L., Barre F.-X., Aroyo M., Stasiak A., Stasiak A.Z., Sherratt D.J.;
RT "FtsK is a DNA motor protein that activates chromosome dimer resolution by
RT switching the catalytic state of the XerC and XerD recombinases.";
RL Cell 108:195-205(2002).
RN [11]
RP FUNCTION, DOMAIN, AND MUTAGENESIS OF LYS-997.
RX PubMed=15522074; DOI=10.1111/j.1365-2958.2004.04335.x;
RA Bigot S., Corre J., Louarn J.M., Cornet F., Barre F.X.;
RT "FtsK activities in Xer recombination, DNA mobilization and cell division
RT involve overlapping and separate domains of the protein.";
RL Mol. Microbiol. 54:876-886(2004).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [13]
RP FUNCTION, DOMAIN, AND INTERACTION WITH XERD.
RC STRAIN=K12 / AB1157;
RX PubMed=16553881; DOI=10.1111/j.1365-2958.2005.05033.x;
RA Yates J., Zhekov I., Baker R., Eklund B., Sherratt D.J., Arciszewska L.K.;
RT "Dissection of a functional interaction between the DNA translocase, FtsK,
RT and the XerD recombinase.";
RL Mol. Microbiol. 59:1754-1766(2006).
RN [14]
RP INTERACTION WITH FTSQ.
RC STRAIN=K12;
RX PubMed=17185541; DOI=10.1099/mic.0.2006/000265-0;
RA D'Ulisse V., Fagioli M., Ghelardini P., Paolozzi L.;
RT "Three functional subdomains of the Escherichia coli FtsQ protein are
RT involved in its interaction with the other division proteins.";
RL Microbiology 153:124-138(2007).
RN [15]
RP REVIEW.
RX PubMed=17511809; DOI=10.1111/j.1365-2958.2007.05755.x;
RA Bigot S., Sivanathan V., Possoz C., Barre F.X., Cornet F.;
RT "FtsK, a literate chromosome segregation machine.";
RL Mol. Microbiol. 64:1434-1441(2007).
RN [16]
RP INTERACTION WITH FTSZ; FTSQ; FTSL AND FTSI.
RC STRAIN=K12;
RX PubMed=18759781; DOI=10.1111/j.1574-6968.2008.01317.x;
RA Grenga L., Luzi G., Paolozzi L., Ghelardini P.;
RT "The Escherichia coli FtsK functional domains involved in its interaction
RT with its divisome protein partners.";
RL FEMS Microbiol. Lett. 287:163-167(2008).
RN [17]
RP FUNCTION.
RX PubMed=18363794; DOI=10.1111/j.1365-2958.2008.06212.x;
RA Kennedy S.P., Chevalier F., Barre F.X.;
RT "Delayed activation of Xer recombination at dif by FtsK during septum
RT assembly in Escherichia coli.";
RL Mol. Microbiol. 68:1018-1028(2008).
RN [18]
RP FUNCTION, AND DOMAIN.
RX PubMed=19246541; DOI=10.1093/nar/gkp104;
RA Bonne L., Bigot S., Chevalier F., Allemand J.F., Barre F.X.;
RT "Asymmetric DNA requirements in Xer recombination activation by FtsK.";
RL Nucleic Acids Res. 37:2371-2380(2009).
RN [19]
RP DOMAIN.
RC STRAIN=K12 / AB1157;
RX PubMed=21091498; DOI=10.1111/j.1365-2958.2010.07412.x;
RA Dubarry N., Possoz C., Barre F.X.;
RT "Multiple regions along the Escherichia coli FtsK protein are implicated in
RT cell division.";
RL Mol. Microbiol. 78:1088-1100(2010).
RN [20]
RP FUNCTION.
RX PubMed=19854947; DOI=10.1093/nar/gkp843;
RA Graham J.E., Sivanathan V., Sherratt D.J., Arciszewska L.K.;
RT "FtsK translocation on DNA stops at XerCD-dif.";
RL Nucleic Acids Res. 38:72-81(2010).
RN [21]
RP FUNCTION.
RX PubMed=20081205; DOI=10.1093/nar/gkp1243;
RA Bigot S., Marians K.J.;
RT "DNA chirality-dependent stimulation of topoisomerase IV activity by the C-
RT terminal AAA+ domain of FtsK.";
RL Nucleic Acids Res. 38:3031-3040(2010).
RN [22]
RP REVIEW.
RX PubMed=20298190; DOI=10.1042/bst0380395;
RA Sherratt D.J., Arciszewska L.K., Crozat E., Graham J.E., Grainge I.;
RT "The Escherichia coli DNA translocase FtsK.";
RL Biochem. Soc. Trans. 38:395-398(2010).
RN [23]
RP REVIEW.
RX PubMed=20922738; DOI=10.1002/cbic.201000347;
RA Crozat E., Grainge I.;
RT "FtsK DNA translocase: the fast motor that knows where it's going.";
RL ChemBioChem 11:2232-2243(2010).
RN [24]
RP FUNCTION, AND DOMAIN.
RX PubMed=21371996; DOI=10.1093/nar/gkr078;
RA Grainge I., Lesterlin C., Sherratt D.J.;
RT "Activation of XerCD-dif recombination by the FtsK DNA translocase.";
RL Nucleic Acids Res. 39:5140-5148(2011).
RN [25]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND MUTAGENESIS OF ASP-135; ASP-136;
RP ILE-137 AND TRP-138.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=25002583; DOI=10.1074/jbc.m114.569624;
RA Berezuk A.M., Goodyear M., Khursigara C.M.;
RT "Site-directed fluorescence labeling reveals a revised N-terminal membrane
RT topology and functional periplasmic residues in the Escherichia coli cell
RT division protein FtsK.";
RL J. Biol. Chem. 289:23287-23301(2014).
RN [26]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 818-1329, 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 [27]
RP STRUCTURE BY NMR OF 1261-1329, AND DNA-BINDING.
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).
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. Stoppage of
CC translocation is accompanied by a reduction in ATPase activity. Also
CC stimulates topoisomerase 4 activity. Required for the targeting of
CC FtsQ, FtsL and FtsI to the septum. {ECO:0000269|PubMed:11703663,
CC ECO:0000269|PubMed:11832210, ECO:0000269|PubMed:15522074,
CC ECO:0000269|PubMed:16553881, ECO:0000269|PubMed:18363794,
CC ECO:0000269|PubMed:19246541, ECO:0000269|PubMed:19854947,
CC ECO:0000269|PubMed:20081205, ECO:0000269|PubMed:21371996,
CC ECO:0000269|PubMed:9723913, ECO:0000269|PubMed:9829960}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA. Interacts with
CC FtsZ, FtsQ, FtsL and FtsI. {ECO:0000269|PubMed:16553881,
CC ECO:0000269|PubMed:16916635, ECO:0000269|PubMed:17185541,
CC ECO:0000269|PubMed:18759781}.
CC -!- INTERACTION:
CC P46889; P0AFG8: aceE; NbExp=2; IntAct=EBI-550795, EBI-542683;
CC P46889; P06136: ftsQ; NbExp=3; IntAct=EBI-550795, EBI-1130157;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11703663,
CC ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:25002583, ECO:0000269|PubMed:9723913}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:11703663,
CC ECO:0000269|PubMed:11948172, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:25002583, ECO:0000269|PubMed:9723913}. Note=Located
CC at the septum. Colocalizes with FtsZ. ZipA, FtsZ and FtsA, but not FtsI
CC and FtsQ are required to target it to the septum.
CC -!- INDUCTION: Induced by DNA-damaging agents.
CC {ECO:0000269|PubMed:9723913}.
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 {ECO:0000269|PubMed:15522074, ECO:0000269|PubMed:16553881,
CC ECO:0000269|PubMed:19246541, ECO:0000269|PubMed:21091498,
CC ECO:0000269|PubMed:21371996, ECO:0000269|PubMed:9829960}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; Z49932; CAA90178.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73976.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35615.1; -; Genomic_DNA.
DR PIR; A64828; A64828.
DR RefSeq; NP_415410.1; NC_000913.3.
DR RefSeq; WP_000076967.1; NZ_LN832404.1.
DR PDB; 2IUS; X-ray; 2.70 A; A/B/C/D/E/F=818-1329.
DR PDB; 2J5P; NMR; -; A=1261-1329.
DR PDB; 5DCF; X-ray; 2.30 A; A=1261-1329.
DR PDBsum; 2IUS; -.
DR PDBsum; 2J5P; -.
DR PDBsum; 5DCF; -.
DR AlphaFoldDB; P46889; -.
DR SMR; P46889; -.
DR BioGRID; 4260652; 497.
DR ComplexPortal; CPX-1936; Divisome complex.
DR DIP; DIP-9703N; -.
DR IntAct; P46889; 7.
DR STRING; 511145.b0890; -.
DR TCDB; 3.A.12.1.2; the septal dna translocator (s-dna-t) family.
DR jPOST; P46889; -.
DR PaxDb; P46889; -.
DR PRIDE; P46889; -.
DR EnsemblBacteria; AAC73976; AAC73976; b0890.
DR EnsemblBacteria; BAA35615; BAA35615; BAA35615.
DR GeneID; 945102; -.
DR KEGG; ecj:JW0873; -.
DR KEGG; eco:b0890; -.
DR PATRIC; fig|511145.12.peg.920; -.
DR EchoBASE; EB3016; -.
DR eggNOG; COG1178; Bacteria.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_0_1_6; -.
DR InParanoid; P46889; -.
DR OMA; DPFWKPG; -.
DR PhylomeDB; P46889; -.
DR BioCyc; EcoCyc:G6464-MON; -.
DR EvolutionaryTrace; P46889; -.
DR PRO; PR:P46889; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0032153; C:cell division site; IC:ComplexPortal.
DR GO; GO:1990586; C:divisome complex; IC:ComplexPortal.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoliWiki.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:EcoliWiki.
DR GO; GO:0003677; F:DNA binding; IDA:EcoliWiki.
DR GO; GO:0015616; F:DNA translocase activity; IDA:EcoCyc.
DR GO; GO:0036121; F:double-stranded DNA helicase activity; IMP:CACAO.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoCyc.
DR GO; GO:0051301; P:cell division; IMP:CACAO.
DR GO; GO:0071236; P:cellular response to antibiotic; IMP:EcoliWiki.
DR GO; GO:0007059; P:chromosome segregation; IDA:EcoliWiki.
DR GO; GO:0000917; P:division septum assembly; IC:ComplexPortal.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IC:ComplexPortal.
DR GO; GO:0043085; P:positive regulation of catalytic activity; IDA:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:EcoliWiki.
DR GO; GO:0006970; P:response to osmotic stress; IMP:EcoliWiki.
DR GO; GO:0009651; P:response to salt stress; IMP:EcoliWiki.
DR GO; GO:0000920; P:septum digestion after cytokinesis; IMP:EcoliWiki.
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..1329
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098257"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25002583"
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000303|PubMed:25002583"
FT TOPO_DOM 45..74
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25002583"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000303|PubMed:25002583"
FT TOPO_DOM 99..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25002583"
FT TRANSMEM 116..132
FT /note="Helical"
FT /evidence="ECO:0000303|PubMed:25002583"
FT TOPO_DOM 133..162
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:25002583"
FT TRANSMEM 163..179
FT /note="Helical"
FT /evidence="ECO:0000303|PubMed:25002583"
FT TOPO_DOM 180..1329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:25002583"
FT DOMAIN 974..1187
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 184..817
FT /note="Linker"
FT REGION 351..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 604..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 688..712
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..849
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..943
FT /note="Alpha"
FT REGION 944..1258
FT /note="Beta"
FT REGION 1259..1329
FT /note="Gamma"
FT COMPBIAS 434..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..781
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 782..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 994..999
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT MUTAGEN 58
FT /note="E->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:10922461"
FT MUTAGEN 80
FT /note="G->A: In Toe44; loss of function under extreme
FT conditions."
FT MUTAGEN 135
FT /note="D->C: Impairs the ability of FtsK to function in
FT cell division. Uncouples invagination of the inner and
FT outer membranes and results in cellular voids."
FT /evidence="ECO:0000269|PubMed:25002583"
FT MUTAGEN 136
FT /note="D->C: Impairs the ability of FtsK to function in
FT cell division. Uncouples invagination of the inner and
FT outer membranes and results in cellular voids."
FT /evidence="ECO:0000269|PubMed:25002583"
FT MUTAGEN 137
FT /note="I->C: Impairs the ability of FtsK to function in
FT cell division. Uncouples invagination of the inner and
FT outer membranes and results in cellular voids."
FT /evidence="ECO:0000269|PubMed:25002583"
FT MUTAGEN 138
FT /note="W->C: Impairs the ability of FtsK to function in
FT cell division. Uncouples invagination of the inner and
FT outer membranes and results in cellular voids."
FT /evidence="ECO:0000269|PubMed:25002583"
FT MUTAGEN 997
FT /note="K->A: Does not activate Xer recombination."
FT /evidence="ECO:0000269|PubMed:15522074"
FT CONFLICT 333..334
FT /note="WA -> CV (in Ref. 1; CAA90178)"
FT /evidence="ECO:0000305"
FT CONFLICT 388..389
FT /note="QP -> HA (in Ref. 1; CAA90178)"
FT /evidence="ECO:0000305"
FT CONFLICT 1101..1103
FT /note="DSM -> GQY (in Ref. 1; CAA90178)"
FT /evidence="ECO:0000305"
FT CONFLICT 1193
FT /note="A -> R (in Ref. 1; CAA90178)"
FT /evidence="ECO:0000305"
FT HELIX 843..845
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 859..872
FT /evidence="ECO:0007829|PDB:2IUS"
FT TURN 873..876
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 879..886
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 888..897
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 904..907
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 910..916
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 923..926
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 931..939
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 948..952
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 955..958
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 965..971
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 976..980
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 981..983
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 986..990
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 997..1009
FT /evidence="ECO:0007829|PDB:2IUS"
FT TURN 1014..1016
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1017..1022
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1025..1027
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1028..1032
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1038..1041
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1046..1069
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1075..1087
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1115..1121
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1123..1144
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1146..1148
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1150..1157
FT /evidence="ECO:0007829|PDB:2IUS"
FT TURN 1161..1163
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1166..1171
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1174..1178
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1183..1190
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1191..1193
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1195..1197
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1203..1207
FT /evidence="ECO:0007829|PDB:2IUS"
FT STRAND 1215..1219
FT /evidence="ECO:0007829|PDB:2IUS"
FT HELIX 1224..1235
FT /evidence="ECO:0007829|PDB:2IUS"
FT TURN 1262..1264
FT /evidence="ECO:0007829|PDB:2J5P"
FT HELIX 1269..1278
FT /evidence="ECO:0007829|PDB:2J5P"
FT STRAND 1281..1283
FT /evidence="ECO:0007829|PDB:2J5P"
FT HELIX 1284..1291
FT /evidence="ECO:0007829|PDB:2J5P"
FT HELIX 1295..1308
FT /evidence="ECO:0007829|PDB:2J5P"
FT STRAND 1316..1322
FT /evidence="ECO:0007829|PDB:2J5P"
SQ SEQUENCE 1329 AA; 146663 MW; ED24BFB464481CFC CRC64;
MSQEYIEDKE VTLTKLSSGR RLLEALLILI VLFAVWLMAA LLSFNPSDPS WSQTAWHEPI
HNLGGMPGAW LADTLFFIFG VMAYTIPVII VGGCWFAWRH QSSDEYIDYF AVSLRIIGVL
ALILTSCGLA AINADDIWYF ASGGVIGSLL STTLQPLLHS SGGTIALLCV WAAGLTLFTG
WSWVTIAEKL GGWILNILTF ASNRTRRDDT WVDEDEYEDD EEYEDENHGK QHESRRARIL
RGALARRKRL AEKFINPMGR QTDAALFSGK RMDDDEEITY TARGVAADPD DVLFSGNRAT
QPEYDEYDPL LNGAPITEPV AVAAAATTAT QSWAAPVEPV TQTPPVASVD VPPAQPTVAW
QPVPGPQTGE PVIAPAPEGY PQQSQYAQPA VQYNEPLQQP VQPQQPYYAP AAEQPAQQPY
YAPAPEQPVA GNAWQAEEQQ STFAPQSTYQ TEQTYQQPAA QEPLYQQPQP VEQQPVVEPE
PVVEETKPAR PPLYYFEEVE EKRAREREQL AAWYQPIPEP VKEPEPIKSS LKAPSVAAVP
PVEAAAAVSP LASGVKKATL ATGAAATVAA PVFSLANSGG PRPQVKEGIG PQLPRPKRIR
VPTRRELASY GIKLPSQRAA EEKAREAQRN QYDSGDQYND DEIDAMQQDE LARQFAQTQQ
QRYGEQYQHD VPVNAEDADA AAEAELARQF AQTQQQRYSG EQPAGANPFS LDDFEFSPMK
ALLDDGPHEP LFTPIVEPVQ QPQQPVAPQQ QYQQPQQPVP PQPQYQQPQQ PVAPQPQYQQ
PQQPVAPQQQ YQQPQQPVAP QQQYQQPQQP VAPQPQDTLL HPLLMRNGDS RPLHKPTTPL
PSLDLLTPPP SEVEPVDTFA LEQMARLVEA RLADFRIKAD VVNYSPGPVI TRFELNLAPG
VKAARISNLS RDLARSLSTV AVRVVEVIPG KPYVGLELPN KKRQTVYLRE VLDNAKFRDN
PSPLTVVLGK DIAGEPVVAD LAKMPHLLVA GTTGSGKSVG VNAMILSMLY KAQPEDVRFI
MIDPKMLELS VYEGIPHLLT EVVTDMKDAA NALRWCVNEM ERRYKLMSAL GVRNLAGYNE
KIAEADRMMR PIPDPYWKPG DSMDAQHPVL KKEPYIVVLV DEFADLMMTV GKKVEELIAR
LAQKARAAGI HLVLATQRPS VDVITGLIKA NIPTRIAFTV SSKIDSRTIL DQAGAESLLG
MGDMLYSGPN STLPVRVHGA FVRDQEVHAV VQDWKARGRP QYVDGITSDS ESEGGAGGFD
GAEELDPLFD QAVQFVTEKR KASISGVQRQ FRIGYNRAAR IIEQMEAQGI VSEQGHNGNR
EVLAPPPFD
