ID A0A1W9JDA2_9PROT Unreviewed; 769 AA.
AC A0A1W9JDA2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:OQW69614.1};
GN ORFNames=BVN34_04720 {ECO:0000313|EMBL:OQW69614.1};
OS Proteobacteria bacterium ST_bin12.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978760 {ECO:0000313|EMBL:OQW69614.1, ECO:0000313|Proteomes:UP000192616};
RN [1] {ECO:0000313|EMBL:OQW69614.1, ECO:0000313|Proteomes:UP000192616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin12 {ECO:0000313|EMBL:OQW69614.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:OQW69614.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MSXP01000004; OQW69614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9JDA2; -.
DR STRING; 1978760.BVN34_04720; -.
DR Proteomes; UP000192616; 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, ECO:0000313|EMBL:OQW69614.1};
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 32..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..194
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 414..623
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 769 AA; 84274 MW; F27C16B87CCE7196 CRC64;
MFLNKKSPAV NGRLQAPPSP SQQHGASLVR EAWWLGLVLV GLYLAVILIS YHNQDPSWSH
MASDNAVIQN AGGAVGAWIA DMLLYLFGFS AWWWVVLAFY SMWLIYLRLE LTISERPFLV
FNLVGFALLL ISSCALEAGH LITLPATLSS TAGGMLGNSV DGALRAMFGF TGSTMLLLLL
FAVGFSLFTG WSWIMMTEKL GKNLIDAYEW TINKYHDWQD RKAGKAVVQK REEFVEAERK
RTEDRAPVEI KAPVIEIAQS ERVQKEKQTT LFTTDLDSSL PPLHLLDEAN NTVELPSAET
LDFTSRLIER KLMDFGIEVK VLSAQPGPVI TRYELEPAAG VKGSQVTNLV KDLARALSVA
SVRVVETIPG KTYMGLEIPN PKRQIVYLSE IMSSQAYASV NSPLAICLGK DIAGKPAVAD
LAKMPHVLVA GTTGSGKSVA INALILSWLY KADASQVRMI LIDPKMLELS VYEGIPHLLA
PVVTDMRQAA NALNWCVNEM ERRYKLMSSL GVRNLAGYNQ KIKDADKAGE KIPHPFSITP
DAPEPLEEMP LIVVVIDELA DLMMVVGKKV EELIARLAQK ARASGIHLVL ATQRPSVDVI
TGLIKANVPT RISFQVSSKI DSRTILDQMG AEALLGQGDM LYMPPGTGYP LRIHGAFVSD
HEVHQVVNHL KAMGEPNYIE GILTNETEGG EAGEFSSDDG AEKDPLYDEA VNIVLTSRRA
SISSVQRQLR IGYNRAARLI EDMERAGLVS AMQSNGNREV LAKGNASTD
//
