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FTSK1_NEIMA
ID   FTSK1_NEIMA             Reviewed;         812 AA.
AC   Q9JU31; A1ISB8;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=DNA translocase FtsK 1;
GN   Name=ftsK1; OrderedLocusNames=NMA1527;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAM08674.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AL157959; CAM08674.1; ALT_INIT; Genomic_DNA.
DR   PIR; C81844; C81844.
DR   RefSeq; WP_002245997.1; NC_003116.1.
DR   AlphaFoldDB; Q9JU31; -.
DR   SMR; Q9JU31; -.
DR   EnsemblBacteria; CAM08674; CAM08674; NMA1527.
DR   KEGG; nma:NMA1527; -.
DR   HOGENOM; CLU_001981_9_7_4; -.
DR   BioCyc; NMEN122587:NMA_RS07615-MON; -.
DR   Proteomes; UP000000626; 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..812
FT                   /note="DNA translocase FtsK 1"
FT                   /id="PRO_0000098272"
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;  87996 MW;  29C572C69AEF4441 CRC64;
     MTEKSHKKTA KGRAGSPSPT SARNKKADNG ARGNKVSERL KAVKELQKTE TKKARPEHVV
     NLIGDALWLM GLAATLYLVI SLISFDMGDP SWSHSSPVVE DVANWGGLFG AYVADVGYYL
     FGWSFWWWIA AACVMLYKNF 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 NPFSLNPDNP EPLEKLPMIV
     VVIDELADLM MTERKAVEQQ IARLAQKARA AGIHMIVATQ RPSVDVVTGL IKANIPTRMA
     FTVQSKIDSR TILDQMGADE LLKYGDSLFL QPGSAEPTRL QGAFVSDDEV HHVVAFVKEQ
     APANYVEGLL TGEAAQETAN IVSPNADSDE LFDQAVAYVL ESKKTSISSL QRQLRIGYNR
     AANLMEALEN AGVVSPSDLN GSRKILAHKD HL
 
 
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