ID C6SEF1_NEIME Unreviewed; 1014 AA.
AC C6SEF1;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 08-NOV-2023, entry version 52.
DE SubName: Full=Putative cell division protein {ECO:0000313|EMBL:CBA08065.1};
GN Name=ftsK3 {ECO:0000313|EMBL:CBA08065.1};
GN ORFNames=NME_1670 {ECO:0000313|EMBL:CBA08065.1};
OS Neisseria meningitidis alpha153.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=663926 {ECO:0000313|EMBL:CBA08065.1};
RN [1] {ECO:0000313|EMBL:CBA08065.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Alpha153 {ECO:0000313|EMBL:CBA08065.1};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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; AM889137; CBA08065.1; -; Genomic_DNA.
DR AlphaFoldDB; C6SEF1; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; 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; 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}; Cell cycle {ECO:0000313|EMBL:CBA08065.1};
KW Cell division {ECO:0000313|EMBL:CBA08065.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}.
FT DOMAIN 662..871
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
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 496..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 679..686
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1014 AA; 110979 MW; 0DA37EBFA4A8B43B 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 EQAQHSRIAE TDHLADDVLN GGWQEETAAI ADDGSEGAAE RSNGQYLSET
EAFGHDSRAV CPFEDVPSER PSCRASDTEA DEGAFPSEET GAVSEHLPTT DLLLPPLFNP
EATQTEEELL ENSITIEEKL AEFKVKVKVV DSYSGPVITR YEIEPDVGVR GNSVLNLEKD
LARSLGVASI RVVETIPGKT CMGLELPNPK RQMIRLSEIF NSPEFAESKS KLTLALGQDI
TGQPVVTDLG KAPHLLVAGT TGSGKSVGVN AMILSMLFKA APEDVRMIMI DPKMLELSIY
EGIPHLLAPV VTDMKLAANA LNWCVNEMEK RYRLMSFMGV RNLAGFNQKI AEAAARGEKI
GNPFSLTPDD PEPLEKLPFI VVVVDEFADL MMTAGKKIEE LIARLAQKAR AAGIHLILAT
QRPSVDVITG LIKANIPTRI AFQVSSKIDS RTILDQMGAE NLLGQGDMLF LPPGTAYPQR
VHGAFASDEE VHRVVEYLKQ FGEPDYVDDI LSGGMSDDLL GISRSGDGET DPMYDEAVSV
VLKTRKASIS GVQRALRIGY NRAARLIDQM EAEGIVSAPE HNGNRTILVP LDNA
//
