ID   FTSK2_NEIMA             Reviewed;        1014 AA.
AC   Q9JUK9; A1IRR0;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=DNA translocase FtsK 2;
GN   Name=ftsK2; OrderedLocusNames=NMA1266;
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}; Single-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; AL157959; CAM08454.1; -; Genomic_DNA.
DR   PIR; H81894; H81894.
DR   RefSeq; WP_002246169.1; NC_003116.1.
DR   AlphaFoldDB; Q9JUK9; -.
DR   SMR; Q9JUK9; -.
DR   PRIDE; Q9JUK9; -.
DR   EnsemblBacteria; CAM08454; CAM08454; NMA1266.
DR   KEGG; nma:NMA1266; -.
DR   HOGENOM; CLU_001981_5_0_4; -.
DR   OMA; WIVMIVI; -.
DR   BioCyc; NMEN122587:NMA_RS06370-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; 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; 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..1014
FT                   /note="DNA translocase FtsK 2"
FT                   /id="PRO_0000098273"
FT   TRANSMEM        1..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          662..871
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          89..142
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          283..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..525
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        120..140
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        294..308
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         682..687
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1014 AA;  111024 MW;  4ABDD41A9402C481 CRC64;
     MFWIVLIVIL LLALAGLFFV RAQSEREWMR EVSAWQEKKG EKQAELPEIK DGMPDFPELA
     LMLFHAVKTA VYWLFVGVVR FCRNYLAHES EPDRPVPPAS ANRADVPTAS DGYSDSGNGT
     EEAETEEAEA AEEEAADTED IATAVIDNRR IPFDRSIAEG LMPSESEISP VRPVFKEITL
     EEATRALNSA ALRETKKRYI DAFEKNETAV PKVRVSDTPM EGLQIIGLDD PVLQRTYSRM
     FDADKEAFSE SADYGFEPYF EKQHPSAFSA VKAENARNAP FRRHAGQGKG QAEAKSPDVS
     QGQSVSDGTA VRDARRRVSV NLKEPNKATV SAEARISRLI PESRTVVGKR DVEMPSETEN
     VFTETVSSVG YGGPVYDETA DIHIEEPAAP DAWVVEPPEV PKVPMPAIDI PPPPPVSEIY
     NRTYEPPAGF EQVQRSRIAE TDHLADDVLN GGWQEETAAI ANDGSEGVAE RSSGQYLSET
     EAFGHDSQAV CPFENVPSER PSRRASDTEA DEGAFQSEET GAVSEHLPTT DLLLPPLFNP
     GATQTEEELL ENSITIEEKL AEFKVKVKVV DSYSGPVITR YEIEPDVGVR GNSVLNLEKD
     LARSLGVASI RVVETILGKT CMGLELPNPK RQMIRLSEIF NSPEFAESKS KLTLALGQDI
     TGQPVVTDLG KAPHLLVAGT TGSGKSVGVN AMILSMLFKA APEDVRMIMI DPKMLELSIY
     EGIPHLLAPV VTDMKLAANA LNWCVNEMEK RYRLMSFMGV RNLAGFNQKI AEAAARGEKI
     GNPFSLTPDN PEPLEKLPFI VVVVDEFADL MMTAGKKIEE LIARLAQKAR AAGIHLILAT
     QRPSVDVITG LIKANIPTRI AFQVSSKIDS RTILDQMGAE NLLGQGDMLF LPPGTAYPQR
     VHGAFASDEE VHRVVEYLKQ FGEPDYVDDI LSGGMSDDLL GISRSGDGET DPMYDEAVSV
     VLKTRKASIS GVQRALRIGY NRAARLIDQM EAEGIVSAPE HNGNRTILVP LDNA