GenomeNet

Database: UniProt
Entry: W6TD61_HOLOB
LinkDB: W6TD61_HOLOB
Original site: W6TD61_HOLOB 
ID   W6TD61_HOLOB            Unreviewed;       720 AA.
AC   W6TD61;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=P618_200976 {ECO:0000313|EMBL:ETZ06863.1};
OS   Holospora obtusa F1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales; Holosporaceae;
OC   Holospora.
OX   NCBI_TaxID=1399147 {ECO:0000313|EMBL:ETZ06863.1, ECO:0000313|Proteomes:UP000019112};
RN   [1] {ECO:0000313|EMBL:ETZ06863.1, ECO:0000313|Proteomes:UP000019112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F1 {ECO:0000313|EMBL:ETZ06863.1,
RC   ECO:0000313|Proteomes:UP000019112};
RX   PubMed=25115770;
RA   Dohra H., Tanaka K., Suzuki T., Fujishima M., Suzuki H.;
RT   "Draft genome sequences of three Holospora species (Holospora obtusa,
RT   Holospora undulata, and Holospora elegans), endonuclear symbiotic bacteria
RT   of the ciliate Paramecium caudatum.";
RL   FEMS Microbiol. Lett. 359:16-18(2014).
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:ETZ06863.1}.
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; AWTR02000080; ETZ06863.1; -; Genomic_DNA.
DR   RefSeq; WP_021827882.1; NZ_AWTR02000080.1.
DR   AlphaFoldDB; W6TD61; -.
DR   STRING; 1399147.P618_200976; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000019112; 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   Coiled coil {ECO:0000256|SAM:Coils};
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:UP000019112};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        105..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        142..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          367..585
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   COILED          436..488
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         384..391
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   720 AA;  80720 MW;  FDB5CB3F20EB18D3 CRC64;
     MAFWKNSSFL SSVSHAVRDG VALLVLAFDF FLLVSFLSYS PHDPSWNICV RGVPDNLMGV
     WGACVSDLFF QWFGLGAWVW VFFGFCVFVS IALGTFVWFW LRWSFLLSVF VSFFSTLFSE
     KFGALLKMYP PGLGTWIKEG KISFWVGAVL CVYGIGCSLG LFLGDEFLKK WIIFFSRLKS
     EKEDAQNMQE HVQGGSTDLK SKKDREPLKI SKLSKIKEEI IRAPSIYLNN PETALPPLEF
     LTRNPGKGLL KTEIAQGSID RLQNVLEEFG IKGKIVNTRP GPVVTLYDLE PAPGVKSSRI
     ISLSDDIARS MSVLSARVAL IPGKNLMGIE LSNVHRHMVY LHDLLNSPFY TDFQGQLGLA
     LGQDIAGQPV IVDLAKMPHL LVAGTTGSGK SVGISSMILS LLYRLSPKQC KLLLIDPKII
     DLTVYDEIPH LIAPVITDHK KALEALKWAV QEMELRYRKM SQLGVRNISG YNQKVQEAKK
     ENQPLTREVQ LGFDSENRPC FQQQVFDTEF LPYIVIIVDE MADLMLVAGK ELEVLIQRLA
     QMARAAGIHL IMATQRPSVD VITGTIKANF PTRLSFQVSS KIDSRTILGE QGAESLLGQG
     DMLYMASAGR VMRIHGPFVS DEEIEKVVNF LKTRGSPEYI NMEIQEEDKI TGELLSQQDA
     LYQKAVAIVY QDRKVSTSYI QRQLQIGYNR AARIIEQMEK EGIISAPNHS GKREILNNTR
//
DBGET integrated database retrieval system