ID E3D5I7_NEIM7 Unreviewed; 812 AA.
AC E3D5I7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:ADO31753.1};
GN Name=ftsK3 {ECO:0000313|EMBL:ADO31753.1};
GN OrderedLocusNames=NMBB_1447 {ECO:0000313|EMBL:ADO31753.1};
OS Neisseria meningitidis serogroup B (strain alpha710).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=630588 {ECO:0000313|EMBL:ADO31753.1, ECO:0000313|Proteomes:UP000006929};
RN [1] {ECO:0000313|EMBL:ADO31753.1, ECO:0000313|Proteomes:UP000006929}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alpha710 {ECO:0000313|Proteomes:UP000006929};
RX PubMed=20709895; DOI=10.1128/JB.00883-10;
RA Joseph B., Schneiker-Bekel S., Schramm-Gluck A., Blom J., Claus H.,
RA Linke B., Schwarz R.F., Becker A., Goesmann A., Frosch M., Schoen C.;
RT "Comparative genome biology of a serogroup B carriage and disease strain
RT supports a polygenic nature of meningococcal virulence.";
RL J. Bacteriol. 192:5363-5377(2010).
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.
CC {ECO:0000256|ARBA:ARBA00024784}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CP001561; ADO31753.1; -; Genomic_DNA.
DR RefSeq; WP_002213324.1; NC_017505.1.
DR AlphaFoldDB; E3D5I7; -.
DR GeneID; 61281502; -.
DR KEGG; nmp:NMBB_1447; -.
DR PATRIC; fig|630588.3.peg.1660; -.
DR HOGENOM; CLU_001981_9_7_4; -.
DR Proteomes; UP000006929; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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 CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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 PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:ADO31753.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 62..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 116..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..670
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 812 AA; 87952 MW; 0D63874082DC5591 CRC64;
MTEKSHKKTA KGRAGSPSPT SARNKKADNG ARGNKVSERL KAVKELQKTE TKKARPEHVV
NLIGDALWLM GLAATLYLAI SLISFDMGDP SWSHSSPVVE DVANWGGLFG AYVADVGYYL
FGWSFWWWIA AACVMLYKNF RLHAKQTENE AYNHKIAAAA LFVLTVFSPV LEYFVLGGKY
ADSLPVGAGG MVGIRVGAVF AWLLGKSGSL LIILVVLLLS LSLLVQISWL EFLNGAGRAV
QNRLSALSGK VMALGKRRPN SKTDGVDTQN TRRMVKEAKN ITAKPVALPE GSSSNRKSVA
VSVAPSPKIQ 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 NPFSLNPDSP EPLEKLPMIV
VVIDELADLM MTERKAVEQQ IARLAQKARA AGIHMIVATQ RPSVDVVTGL IKANIPTRMA
FTVQSKIDSR TILDQMGADE LLKYGDSLFL QPGSAEPTRL QGAFVSDDEV HQVVNYVKSQ
APADYIEGLL SGEAALETAN IVNPNADSDE LFDQAVAYVL ESKKTSISSL QRQLRIGYNR
AANLMEALEN AGVVSPTDLN GSRKILAHKD HL
//
