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Database: UniProt
Entry: A0A1H7T5N6_9BURK
LinkDB: A0A1H7T5N6_9BURK
Original site: A0A1H7T5N6_9BURK 
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}.
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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
//
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