ID   F0Q963_PARA1            Unreviewed;       779 AA.
AC   F0Q963;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Cell division protein FtsK/SpoIIIE {ECO:0000313|EMBL:ADX47193.1};
GN   OrderedLocusNames=Acav_3291 {ECO:0000313|EMBL:ADX47193.1};
OS   Paracidovorax avenae (strain ATCC 19860 / DSM 7227 / CCUG 15838 / JCM 20985
OS   / LMG 2117 / NCPPB 1011) (Acidovorax avenae).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=643561 {ECO:0000313|EMBL:ADX47193.1, ECO:0000313|Proteomes:UP000002482};
RN   [1] {ECO:0000313|Proteomes:UP000002482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19860 / DSM 7227 / CCUG 15838 / JCM 20985 / LMG 2117 /
RC   NCPPB 1011 {ECO:0000313|Proteomes:UP000002482};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Chertkov O., Held B., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Gordon S., Woyke T.;
RT   "Complete sequence of Acidovorax avenae subsp. avenae ATCC 19860.";
RL   Submitted (FEB-2011) 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}.
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DR   EMBL; CP002521; ADX47193.1; -; Genomic_DNA.
DR   RefSeq; WP_013595681.1; NC_015138.1.
DR   AlphaFoldDB; F0Q963; -.
DR   GeneID; 34235662; -.
DR   KEGG; aaa:Acav_3291; -.
DR   HOGENOM; CLU_001981_9_7_4; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000002482; Chromosome.
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:ADX47193.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000002482};
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..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          423..632
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          699..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         440..447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   779 AA;  84595 MW;  E37D3FEB8ACBCC37 CRC64;
     MTYSLNTLNA SAGGRSAPRS MAARFGHEIG LVVGLLALVF WLLALASYSA QDAAWSTSGA
     HDSRLMANWA GRLGAWLADS SYFALGFSVW WCVAAGVRAW IASLARWMRG GESATPGQSP
     LARRLMFWSG LALLLCASTA LEWSRLYRLE PLLPGHAGGV LGYITGPAGV KWLGFTGSGL
     VAVIAVVAGA ALVFRFSWGQ LAERLGGRID GLVQFGRASR EKARDVAVGK RAAREREEVV
     QEERHEIQEH HPQPVQIIEP VLMADAPPSA RVVKERQKPL FTEMPDSRLP QVDLLDGAQV
     RQETVAPETL EMTSRLIEKK LKDFGVEVRV VAAMPGPVIT RYEIEPATGV KGSQIVNLAK
     DLARSLSLVS IRVIETIPGK NYMALELPNA KRQSIRLSEI LGSQIYHEAK SMLTMGLGKD
     IVGNPVVADL AKMPHVLVAG TTGSGKSVGI NAMILSLLYK AEARDVRLLM IDPKMLEMSV
     YEGIPHLLAP VVTDMKQAAH GLNWCVAEME RRYKLMSKLG VRNLAGYNTK IDEAKAREEF
     IYNPFSLTPE EPEPLERLPH IVVIIDELAD LMMVVGKKIE ELIARLAQKA RAAGIHLILA
     TQRPSVDVIT GLIKANIPTR IAFSVGSKID SRTILDQMGA EALLGMGDML YMASGTGLPI
     RVHGAFVSDD EVHRVVSYLK SQGEPDYIEG VLEGGTVEGD DGAFGEGGGG GEGGEKDPMY
     DQAVEVVLKD RKASISYVQR KLRIGYNRSA RLLEDMEKAG LVSALTASGQ REVLVPHRE
//