ID A0A2V3W4W7_9PROT Unreviewed; 766 AA.
AC A0A2V3W4W7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:PXW89030.1};
GN ORFNames=C8R34_10510 {ECO:0000313|EMBL:PXW89030.1};
OS Nitrosomonas sp. Nm84.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=200124 {ECO:0000313|EMBL:PXW89030.1, ECO:0000313|Proteomes:UP000248024};
RN [1] {ECO:0000313|EMBL:PXW89030.1, ECO:0000313|Proteomes:UP000248024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm84 {ECO:0000313|EMBL:PXW89030.1,
RC ECO:0000313|Proteomes:UP000248024};
RA Wagner M.;
RT "Active sludge and wastewater microbial communities from Klosterneuburg,
RT Austria.";
RL Submitted (MAY-2018) 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 -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
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:PXW89030.1}.
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DR EMBL; QJJP01000005; PXW89030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2V3W4W7; -.
DR Proteomes; UP000248024; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000248024};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..619
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 427..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 766 AA; 84669 MW; D67ED16B7765EEA0 CRC64;
MNLMNKPMAK KSSGQSFSPK VARLLRESVC LVLTGAALYL ILIFFSYDRD DAGWSHSGDL
NPIQNAGGHA GAWLADLLLF LFGASAWWWV AFFLSAVAWS YRRIDIAGIF DRHSLLLTAG
GFLLLLSASS GLESLRFHTI SISLPLMPGG MLGDAISYHL SKILGFTGAT LTLLIFIAIG
FSQFTGLSWV RFVEKIGENI ETFLFFMKET WETRQDKFAG IIASRVREEI VESEKKRIEE
MPQLHIELPT TTIIKSQRII KEKQTPLFSD LPDSPLPPLH LLDEPEKDFE VLSKETLEFT
SRLIERKLKE FGVDVKVVAA FPGPVITRYE IEPAVGVKGN QVINLVKDLA RALSVASIRV
VETIPGKTSM GLELPNPKRQ VVRLQEILSS QAYADSASPL TIALGKDISG RPIVSDLAKM
PHALVAGTTG SGKSVAINAV ILSLIYKATP EQTRLILIDP KMLELSVYEG IPHLLTPVVT
DMREAASALR WCVAEMERRY KLMSALGVRN LGGYNQKIQE AIKKEEPVVN PFSPPEEPPE
YLEELPLIVV VIDELADLMM VVGKKVEHLI ARLAQKARAS GIHLLLATQR PSVDVITGLI
KANIPTRIAF QVSSKIDSRT ILDQMGAEAL LGQGDMLYLP PGSGYPQRIH GAFVADHEVH
KVVEYLKEHG EPCYIEEILR IDDEENDAGS TLEIKKSTEG EADPLYDEAV AIVVKTRRAS
ISLVQRNLRI GYNRAARLIE EMERAGLVSS MQSNGNREVL APSRSE
//