FTSK_HAEDU
ID FTSK_HAEDU Reviewed; 957 AA.
AC P59836;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=HD_1476;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases.
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; AE017143; AAP96278.1; -; Genomic_DNA.
DR AlphaFoldDB; P59836; -.
DR SMR; P59836; -.
DR STRING; 233412.HD_1476; -.
DR EnsemblBacteria; AAP96278; AAP96278; HD_1476.
DR KEGG; hdu:HD_1476; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_7_0_6; -.
DR OMA; DMLYSGA; -.
DR Proteomes; UP000001022; 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..957
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098260"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 174..957
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 607..820
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 627..632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 957 AA; 105998 MW; C402C678875330B8 CRC64;
MTVIERFKSN LKGKQNLINF GFILIGLFGC YLLIAWASYS PLDNAWSTAS SVTHDTVLNK
TGKLGAWLID LLYAFLGNVA FVVPFVLFSF AIYALIFRIA EQWKWRNLLL QIGSFILLLI
GLSGIASVLL PNSAYYLAGG FVGGMLQSLL NGIIGQVGLL LLSTVLMSIG FYFCSGQLLF
SLGIQFYQWL FIKKPQSNTI LEAANPHLNA QNNETTKSIV ANPSENAHVD QLVTHENATE
QLTDVSAFTR PTIHGLKSSS TLNTDKTKYN QVNAQPLTDP MMFKIEKKVI LPKINMQHPE
NELTNLSMEQ TNSIDNLEIR LPKVHLNTAV TNPEIKTVEH HAQNRPLEMP TQIQPVFDQP
ITPTISLNVE DQPLDIESNE AQLAEEFAAA EQMRLANMEQ RAKAEGLEET FNQIITSPTL
TVSINESSEQ PTEKDLNPTH HDNGANYPKG YGKTLLHPLL QRNNVVEKPT TPLPTLELLA
KNPVQTQQIT EQEIFDTSHR LENALANYNV KATVEDVLVG PVVTRYEIKP AAGIKANKVT
ALANDLAREL MFKAIRITEV VPGKPYMGIE TPNTHRQTVW LRDVLDSEAF RHTQATLPMA
LGKDISGQPI VVDMAKMPHL LVAGQTGGGK SVGINTMILS LLFKLTPEQV RFIMIDPKVV
ELSVYNDIPH LLTPVVTDMK KAANALRWAV GEMERRYLLI SHLQVRNIEG YNDKIDQASA
MNFPIPDPTW RPADSIGQLP PPLTKLSYIV LIVDEFADLI MSAGKEVEEY IMRIAQKARA
VGIHLILATQ RPSTDVITGV IKANIPSRIA FTVASQIDSR TILDAGGAEA LLGRGDMLYS
ASGSPEIMRI HGAFMSDEEV QRIADNWRAR GKPQYLDSVV ASHEDENDSR TNTITELDPL
FDEIVAYVIE SGVTSISGIQ RRFSLGFNRA GRIIDQMEAQ AIISEPGKGG KREVLAR
