FTSK_ECOL6
ID FTSK_ECOL6 Reviewed; 1347 AA.
AC Q8FJC7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=c1027;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN79499.1; -; Genomic_DNA.
DR RefSeq; WP_000077100.1; NC_004431.1.
DR AlphaFoldDB; Q8FJC7; -.
DR SMR; Q8FJC7; -.
DR STRING; 199310.c1027; -.
DR EnsemblBacteria; AAN79499; AAN79499; c1027.
DR KEGG; ecc:c1027; -.
DR eggNOG; COG1178; Bacteria.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_0_1_6; -.
DR OMA; DPFWKPG; -.
DR BioCyc; ECOL199310:C1027-MON; -.
DR Proteomes; UP000001410; 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 Transmembrane; Transmembrane helix.
FT CHAIN 1..1347
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098259"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 45..74
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 75..98
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 99..115
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 116..132
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 133..162
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TRANSMEM 163..179
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT TOPO_DOM 180..1347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P46889"
FT DOMAIN 992..1205
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 354..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..486
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 664..681
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..716
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 754..773
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 784..833
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 1012..1017
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1347 AA; 148940 MW; 7146219221FEC788 CRC64;
MSQEYTEDKE 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 RMDDEEEITY TARGVAADPD DVLFSGNRAT
QPEYDEYDPL LNGAPITEPV AVAAAATTAT QSWAAPVEPV TQTPPVASVD VPPTQPTVAW
QPVPGPQTGE PVIAPAPEGY PHQSQYAQPA VQYNEPLQQP VQPQQPYYAP AAEQPVQQPY
YAPAAEQPVQ QPYYAPAPEQ PVAGNAWQAE EQQSTFAPQS TYQTEQTYQQ PAAQEPLYQQ
PQPVEQQPVV EPEPVVEETK PTRPPLYYFE EVEEKRARER EQLAAWYQPI PEPVKEPEPI
KSSLKAPSVA AVPPVEAAAA VSPLASGVKK ATLATGAAAT VAAPVFSLAN SGGPRPQVKE
GIGPQLPRPK RIRVPTRREL ASYGIKLPSQ RAAEEKAREA QRNQYDSGDQ YNDDEIDAMQ
QDELARQFAQ TQQQRYGEQY QHDVPVNTED ADAAAEAELA RQFAQTQQQR YSGEQPAGAN
PFSLDDFEFS PMKALLDDGP HEPLFTPIVE PVQQPQQPVA PQQQYQQPQQ PVAPQPQYQQ
PQQPVAPQPQ YQQPQYQQPQ QPVAPQQQYQ QPQQPVTQQP QYQQPQQPVV PQPQDTLLHP
LLMRNGDSRP LHKPTTPLPS LDLLTPPPSE VEPVDTFALE QMARLVEARL ADFRIKADVV
NYSPGPVITR FELNLAPGVK AARISNLSRD LARSLSTVAV RVVEVIPGKP YVGLELPNKK
RQTVYLREVL DNAKFRDNPS PLTVVLGKDI AGEPVVADLA KMPHLLVAGT TGSGKSVGVN
AMILSMLYKA QPEDVRFIMI DPKMLELSVY EGIPHLLTEV VTDMKDAANA LRWCVNEMER
RYKLMSALGV RNLAGYNEKI AEADRMMRPI PDPYWKPGDS MDAQHPVLKK EPYIVVLVDE
FADLMMTVGK KVEELIARLA QKARAAGIHL VLATQRPSVD VITGLIKANI PTRIAFTVSS
KIDSRTILDQ AGAESLLGMG DMLYSGPNST LPVRVHGAFV RDQEVHAVVQ DWKARGRPQY
VDGITSDSES EGGVGGFDGA EELDPLFDQA VQFVTEKRKA SISGVQRQFR IGYNRAARII
EQMEAQGIVS EQGHNGNREV LAPPPFD
