ID A0A1H7T5N6_9BURK Unreviewed; 540 AA.
AC A0A1H7T5N6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:SEL80151.1};
GN ORFNames=SAMN05192542_11439 {ECO:0000313|EMBL:SEL80151.1};
OS Paraburkholderia caballeronis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416943 {ECO:0000313|EMBL:SEL80151.1, ECO:0000313|Proteomes:UP000199120};
RN [1] {ECO:0000313|Proteomes:UP000199120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 26416 {ECO:0000313|Proteomes:UP000199120};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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; FOAJ01000014; SEL80151.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7T5N6; -.
DR STRING; 416943.SAMN05445871_2742; -.
DR Proteomes; UP000199120; Unassembled WGS sequence.
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 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; 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; 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000199120}.
FT DOMAIN 186..395
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 540 AA; 57871 MW; 4AF00C26AE3218ED CRC64;
MIAEQPPTTA TPGSEPGEPT PAPAEAAPRP VVRGHAPTTF EFRPPAASAV ELPGLDLLDR
ASSEIEPISE EKLAQTGQLI EQRLQEFKVP VAVVGASAGP VITRFEIEPA LGVRGSQIVG
LMKDLSRGLG LTSIRVVETI PGKTCMGLEL PNARRQMIRL SEILESGPYQ RSPSKLTIAM
GKDIVGLPVV TDLAKAPHML VAGTTGSGKS VAINAMILSL LYKATPAEVR LIMIDPKMLE
LSVYEGIPHL LAPVVTDMKL AANALNWCVG EMEKRYRLMS AVGVRNLAGF NQKIRDAQAH
EKKIGNPFSL TPDDPEPLST LPMIVVVIDE LADLMMVAGK KIEELIARLA QKARAAGIHL
ILATQRPSVD VITGLIKANI PTRVAFQVSS KIDSRTILDQ MGAESLLGQG DMLFLPPGTG
YPQRVHGAFV ADEEVHSVVE YLKQFGEPEY IEGILDGPAT EGAQQDLFGE TPDAEADPLY
DEAVAFVVRT RRASISSVQR QLRIGYNRAA RLVEQMEAAG LVSPMGINGS REVLAPGAAE
//