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Database: UniProt
Entry: D0W159_NEICI
LinkDB: D0W159_NEICI
Original site: D0W159_NEICI 
ID   D0W159_NEICI            Unreviewed;       810 AA.
AC   D0W159;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   27-MAR-2024, entry version 69.
DE   SubName: Full=FtsK/SpoIIIE family protein {ECO:0000313|EMBL:EEZ72447.1};
GN   ORFNames=NEICINOT_03378 {ECO:0000313|EMBL:EEZ72447.1};
OS   Neisseria cinerea ATCC 14685.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=546262 {ECO:0000313|EMBL:EEZ72447.1, ECO:0000313|Proteomes:UP000003294};
RN   [1] {ECO:0000313|EMBL:EEZ72447.1, ECO:0000313|Proteomes:UP000003294}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14685 {ECO:0000313|EMBL:EEZ72447.1,
RC   ECO:0000313|Proteomes:UP000003294};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEZ72447.1}.
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DR   EMBL; ACDY02000002; EEZ72447.1; -; Genomic_DNA.
DR   RefSeq; WP_003675178.1; NZ_ACDY02000002.1.
DR   AlphaFoldDB; D0W159; -.
DR   STRING; 546262.NEICINOT_03378; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000003294; Unassembled WGS sequence.
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};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          459..668
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         476..483
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   810 AA;  88013 MW;  5A50FB5091E2B9C0 CRC64;
     MTEKSNKKIT KGRAANQSQN SSRKKDNGAR GNKVSEQLKA AKELQKTEAK KARPEHVVNL
     IADALWLMGL AATLYMTISL ISFDMGDPSW SRSSPVVEDA TNWGGLFGAY IADVGYYLFG
     WSFWWWIVAA CVMLYKNFRL HAKPALPGSY NHKIAVAALF ILTVFSPVLE YFVLGGKYSE
     SLPVGAGGMV GIRVGAIFAW LLGKSGSLLI ILVVLLLSVS LLVQVSWLEV LNGTSRTIQN
     CLAVSGRKIS SLGKRRPNTK KDSVDTLNTR RMVKEAKNIT AKPVVSLEGS TSNRKSVAVS
     VAPPPKIQAS LFEDNEVQSN GEYHKPALNL LRLPDNEPVS INPAELERTA ELIESKLAEF
     GIGVQVVSAT SGPVITRYEI EPAQGIKGSQ IVALSKDLAR SMSLQSVRIV ETIAGKNTMG
     IELPNDKRQD VMLSEILSSP VFTEAKSKLT VALGKDIAGT PVVGDLAKMP HLLVAGMTGS
     GKSVGVNGMI MSMLFKATPE EVRFIMIDPK MLELSIYDGI PHLLCPVVTD MREAGQALNW
     CVAEMEKRYR LLSHAGVRNL EGFNQKVEAA KAAGKPLLNP FSLSPDNPEP LEKLPLIVVV
     IDELADLMMT ERKSVEQQIA RLAQKARAAG IHMIVATQRP SVDVVTGLIK ANIPTRMAFT
     VQSKIDSRTI LDQMGADELL KYGDSLFLQP GSAEPTRLQG AFVSDDEVHQ VVNYVKSQAP
     ADYVEGLLSG EAALETTNIV NPNAGSDELF DQAVAYILES KKTSISSLQR QLRIGYNRAA
     NLMEALENAC VVSPADMNGS RKILAHKDHL
//
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