ID W0V496_9BURK Unreviewed; 769 AA.
AC W0V496;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=DNA translocase ftsK {ECO:0000313|EMBL:CDG82082.1};
GN Name=ftsK {ECO:0000313|EMBL:CDG82082.1};
GN ORFNames=GJA_1429 {ECO:0000313|EMBL:CDG82082.1};
OS Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG82082.1, ECO:0000313|Proteomes:UP000027604};
RN [1] {ECO:0000313|EMBL:CDG82082.1, ECO:0000313|Proteomes:UP000027604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA Graupner K., Lackner G., Hertweck C.;
RT "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT agaricidamnosum.";
RL Genome Announc. 3:e00277-e00277(2015).
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; HG322949; CDG82082.1; -; Genomic_DNA.
DR AlphaFoldDB; W0V496; -.
DR STRING; 1349767.GJA_1429; -.
DR KEGG; jag:GJA_1429; -.
DR PATRIC; fig|1349767.4.peg.3133; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_4; -.
DR Proteomes; UP000027604; Chromosome I.
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:UP000027604};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 60..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 161..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 413..622
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 430..437
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 769 AA; 84558 MW; DB03FAB4999DF062 CRC64;
MTERQPLPNR LVRLLSEARW FALAAFGLYF VLILMSFNKA DPGWSHANMV PKVSNLGGRA
GAWLSDLLLF IFGFSAWWWC VWLLRTVWNG YRRLTRKFLL EKTDADDEHQ HEFIIRAIGF
VVMFIGSMGL EFLRLSKTLH VQLPREPGGV LGQLIGHSAH VAFGFTGATL LLLLLFFLGF
SLFFHVSWLS VAERIGGAIE DSIEWVVLRY QDREDRRQGE VAAVKRDEVV VIERAKHVEK
HVAAPPVKIE PQIVTVVKSE RVEKERQAHL FESPGDSRLP PLSLLDEAPP VVETVSVETL
EFTSRLIEKK LSDFGVDAKV VAAYPGPVVT RYEIEPATGV KGSQIVGLAR DLARSLSLTS
IRVVETIPGK NYMALELPNT KRQIVRLTEI LGSKVYNDGV SSLTIALGKD IAGKPVVADL
AKMPHLLVAG TTGSGKSVGI NATILSLLYK SDPLDVRLIL IDPKMLEMSV YEGIPHLLAP
VVTDMRQAGH ALNWAVNEME RRYKLMSKLG VRNLAGYNAK IAESQKKEEH IPNPFSLTPD
APEPLEKLPT IVIIIDELAD LMMVVGKKVE ELIARIAQKA RAAGLHLILA TQRPSVDVIT
GLIKANIPTR IAFQVSSKID SRTILDQMGA ETLLGMGDML YMPPGTGLPV RVHGAFVSDE
EVHRVVKHLQ SQGEPNYVEG ILEGGTLEEG GAEGGAPGEG GGEADALYDQ AVAIVLKNRR
ASISLVQRHL RIGYNRAARL LEQMENSGVV SSMQSNGNRE ILVPAASAE
//