FTSK1_NEIMB
ID FTSK1_NEIMB Reviewed; 812 AA.
AC Q9JZ36;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=DNA translocase FtsK 1;
GN Name=ftsK1; OrderedLocusNames=NMB1314;
OS Neisseria meningitidis serogroup B (strain MC58).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC58;
RX PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA Moxon E.R., Rappuoli R., Venter J.C.;
RT "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT MC58.";
RL Science 287:1809-1815(2000).
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; AE002098; AAF41689.1; -; Genomic_DNA.
DR PIR; A81096; A81096.
DR RefSeq; NP_274333.1; NC_003112.2.
DR RefSeq; WP_002225165.1; NC_003112.2.
DR AlphaFoldDB; Q9JZ36; -.
DR SMR; Q9JZ36; -.
DR STRING; 122586.NMB1314; -.
DR PaxDb; Q9JZ36; -.
DR PRIDE; Q9JZ36; -.
DR EnsemblBacteria; AAF41689; AAF41689; NMB1314.
DR KEGG; nme:NMB1314; -.
DR PATRIC; fig|122586.8.peg.1648; -.
DR HOGENOM; CLU_001981_9_7_4; -.
DR OMA; WEVMAFE; -.
DR Proteomes; UP000000425; 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..812
FT /note="DNA translocase FtsK 1"
FT /id="PRO_0000098274"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..812
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 461..670
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 481..486
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 812 AA; 87958 MW; 0F5894CAD3704BB6 CRC64;
MTEKSHKKTA KGRAGSPSPT SARNKKADNG ARGNKVSERL KAVKELQKTE TKKARPEHVV
NLIGDALWLM GLAATLYLAI SLISFDMGDP SWSHSSPVVE DVANWGGLFG AYVADVGYYL
FGWSFWWWIA AACVVLYKNF RLHAKQTENE AYNHKIAAAA LFVLTVFSPV LEYFVLGGKY
ADSLPVGAGG MVGIRVGAVF AWLLGKSGSL LIILVVLLLS LSLLVQISWL EFLNGAGRAV
QNRLSALSGK VMALGKRRPN TKTDGVDTQN TRRMVKEAKN ITAKPVALPE GSSSNRKSVA
VSVAPPPKIQ VSLFEDDEPR QAGEYHKPTL NLLRIPDSEP VSINPAELER TAELIESKLA
EFGIGVQVVS ATSGPVITRY EIEPAQGVKG SQIVALSKDL ARSMSLQSVR IVETIAGKNT
MGIELPNDKR QDVMLSEILS SPVFAEAKSK LTVALGKDIA GTPVVGDLAK MPHLLVAGMT
GSGKSVGVNG MIMSMLFKAT PDEVRFIMID PKMLELSIYD GIPHLLCPVV TDMREAGQAL
NWCVAEMEKR YRLLSHAGVR NLEGFNQKVE AAKAAGKPLL NPFSLNPDEP EPLEKLPLIV
VVIDELADLM MTERKAVEQQ IARLAQKARA AGIHMIVATQ RPSVDVVTGL IKANIPTRMA
FTVQSKIDSR TILDQMGADE LLKYGDSLFL QPGSAEPTRL QGAFVSDDEV HQVVNYVKSQ
APADYIEGLL SGEAALETAN IVNPNADSDE LFDQAVAYVL ESKKTSISSL QRQLRIGYNR
AANLMEALEN AGVVSSTDLN GSRKILAHKD HL
