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Database: UniProt
Entry: Q2YLQ7_BRUA2
LinkDB: Q2YLQ7_BRUA2
Original site: Q2YLQ7_BRUA2 
ID   Q2YLQ7_BRUA2            Unreviewed;       531 AA.
AC   Q2YLQ7;
DT   20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   OrderedLocusNames=BAB1_1895 {ECO:0000313|EMBL:CAJ11851.1};
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ11851.1, ECO:0000313|Proteomes:UP000002719};
RN   [1] {ECO:0000313|EMBL:CAJ11851.1, ECO:0000313|Proteomes:UP000002719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308 {ECO:0000313|EMBL:CAJ11851.1,
RC   ECO:0000313|Proteomes:UP000002719};
RX   PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG   Microbial Genomics Group;
RG   Lawrence Livermore National Laboratory;
RG   and the Genome Analysis Group;
RG   Oak Ridge National Laboratory;
RA   Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; AM040264; CAJ11851.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2YLQ7; -.
DR   STRING; 359391.BAB1_1895; -.
DR   KEGG; bmf:BAB1_1895; -.
DR   HOGENOM; CLU_001981_9_10_5; -.
DR   Proteomes; UP000002719; Chromosome I.
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: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; 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}; Cell cycle {ECO:0000313|EMBL:CAJ11851.1};
KW   Cell division {ECO:0000313|EMBL:CAJ11851.1};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000002719}.
FT   DOMAIN          166..385
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          445..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         183..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   531 AA;  57991 MW;  A9C448234DE704BA CRC64;
     MEQTAPSPKP GPRAQREAQP SFLKDNGIFE MPSLHFLAEP KLVQRDPALS KDALEQNARL
     LEGVLEDFGV RGEIINVKPG PVVTLYELEP APGIKSSRVI GLADDIARSM SAIAARVAVI
     PGRNAIGIEL PNPKREMVYL REMLASRDFE QSKAKLALAL GKTINGEPVI ADIAKMPHVL
     VAGTTGSGKS VAINTMILSL LYRMTPQEFR LIMIDPKMLE LSVYDGIPHL LTPVVTDPKK
     AVVALKWTVR EMEDRYRKMS KVGVRNIDGF NQRVGLAQKK GEPIARTVQT GFDRNTGEAI
     YETEELDLEP MPYIVVIIDE MADLMMVAGK DIEGAVQRLA QMARAAGIHV IMATQRPSVD
     VITGTIKANF PTRISFQVTS KIDSRTILGE QGAEQLLGQG DMLFMAGGGR IQRVHGPFVG
     DDEVERIVQH LKLQGVPEYL DAITEDEDDD EGGSGPAGTG NLEDSDDPYD QAVAVVLRDK
     KASTSYIQRR LGIGYNRAAS IIERMEDEGI VGPANHAGKR EILVPTGDDD F
//
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