ID E3D4L1_NEIM7 Unreviewed; 1010 AA.
AC E3D4L1;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Cell-division protein FtsK {ECO:0000313|EMBL:ADO31543.1};
GN Name=ftsK1 {ECO:0000313|EMBL:ADO31543.1};
GN OrderedLocusNames=NMBB_1198 {ECO:0000313|EMBL:ADO31543.1};
OS Neisseria meningitidis serogroup B (strain alpha710).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=630588 {ECO:0000313|EMBL:ADO31543.1, ECO:0000313|Proteomes:UP000006929};
RN [1] {ECO:0000313|EMBL:ADO31543.1, 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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CP001561; ADO31543.1; -; Genomic_DNA.
DR RefSeq; WP_014575350.1; NC_017505.1.
DR AlphaFoldDB; E3D4L1; -.
DR KEGG; nmp:NMBB_1198; -.
DR PATRIC; fig|630588.3.peg.1394; -.
DR HOGENOM; CLU_001981_5_0_4; -.
DR Proteomes; UP000006929; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; 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; 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; 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 658..867
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 89..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 284..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 493..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 107..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..140
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 675..682
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1010 AA; 110516 MW; 2BB560AE41F0EFC2 CRC64;
MFWIVMIVIL LLALAGLFFV RAQSEREWMR EVSAWQEKKG EKQAELPEIK DGMPDFPELA
LMLFHAVKTA VYWLFVGVVR FCRNYLAHES EPDRPVPPAS ANRADVPNAS DGYSDSGNGT
EEAETEAAEA AEEEAADTED IATAVIDNRR IPFDRSIAEG LMPSESEISP VRPVFKEITL
EEATRALNGA ALRETKKRYI DAFEKNETAV PKVRVSDTPM EGLQIIGLDD PVLQRTYSRM
FDADKEAFSE SADYGFEPYF EKQHPSAFSA VKAENARNAP FRRHAGQAEA KSPDVSQGQS
VSDGTAVRDA CRRVSVNLKE PNKATVSAEA RISRLIPESR TVVGKRDVEM PSETENVFTE
TVSSVGYGGP VYDETADIHI EEPAAPDAWV VEPPEVPKVP MPAIDIPPPP PVSEIYNRTY
EPPSGFEQVQ RSRIAETDHL ADDVLNGGWQ EETAAIADDG SEGAAERSSG QYLSETEAFG
HDSQAVCPFE NVPSERPSCR VSDTEADEGA FPSEETGAVS EHLPTTDLLL PPLFNPEATQ
TEEELLENSI TIEEKLAEFK VKVKVVDSYS GPVITRYEIE PDVGVRGNSV LNLEKDLARS
LGVASIRVVE TILGKTCMGL ELPNPKRQMI RLSEIFNSPE FAESKSKLTL ALGQDITGQP
VVTDLGKAPH LLVAGTTGSG KSVGVNAMIL SMLFKAAPED VRMIMIDPKM LELSIYEGIP
HLLAPVVTDM KLAANALNWC VNEMEKRYRL MSFMGVRNLA GFNQKIAEAA ARGEKIGNPF
SLTPDDPEPL EKLPFIVVVV DEFADLMMTA GKKIEELIAR LAQKARAAGI HLILATQRPS
VDVITGLIKA NIPTRIAFQV SSKIDSRTIL DQMGAENLLG QGDMLFLPPG TAYPQRVHGA
FASDEEVHRV VEYLKQFGEP DYVDDILSGG GSEELPGIGR SGDDETDPMY DEAVSVVLKT
RKASISGVQR ALRIGYNRAA RLIDQMEAEG IVSAPEHNGN RTILVPLDNA
//
