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Database: UniProt
Entry: A0A0Q8BCI5_9BURK
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ID   A0A0Q8BCI5_9BURK        Unreviewed;       796 AA.
AC   A0A0Q8BCI5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KQZ99170.1};
GN   ORFNames=ASD71_20000 {ECO:0000313|EMBL:KQZ99170.1};
OS   Achromobacter sp. Root565.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=1736564 {ECO:0000313|EMBL:KQZ99170.1, ECO:0000313|Proteomes:UP000052040};
RN   [1] {ECO:0000313|EMBL:KQZ99170.1, ECO:0000313|Proteomes:UP000052040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root565 {ECO:0000313|EMBL:KQZ99170.1,
RC   ECO:0000313|Proteomes:UP000052040};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQZ99170.1, ECO:0000313|Proteomes:UP000052040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root565 {ECO:0000313|EMBL:KQZ99170.1,
RC   ECO:0000313|Proteomes:UP000052040};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQZ99170.1}.
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DR   EMBL; LMGO01000005; KQZ99170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8BCI5; -.
DR   Proteomes; UP000052040; Unassembled WGS sequence.
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: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:KQZ99170.1};
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};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        78..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          435..644
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         452..459
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   796 AA;  86152 MW;  7C84732164153112 CRC64;
     MSRMPRISTA SPRASRNTRN GPSPLQTRIS ALLREARWIL FAALAAWLTL VLATWSASDP
     GWSHSVPGDV VRNQGGRLGA YLADILLYLF GFSAWWWVIL LLHRVRAGYR RLAAQLRVAN
     SKQPEVLPRV HWEEGIGFVL LMVGSLGMEA LRLASRGTHL PGASETASGA GGVIGQMLAG
     LIGSSIGFTG ATLAFLVMLA IGLSLFFSFS WLAVAERVGS WLEGLVRKMR NSYTARQDRK
     VGEVAKAVRT EQVVAKQEKL VHEQPVRIEP AITVVPKSER VEKEKQQSLF FPPTGGAEGD
     LPAISLLDPP LNNQETVSAE TIEFTSRLIE KKLADFGVSV TVVAAQAGPV ITRYEIEPAT
     GVKGSQIVNL AKDLARALSL VSIRVVETIP GKNLMGLELP NPRRQMVRLS EILGSQTYHA
     SHSVVTMALG KDIAGNPVVA DLAKMPHLLV AGTTGSGKSV GINAMILSLL YKADASHTRL
     ILIDPKMLEM SVYEGIPHLL APVVTDMRHA SNALNWCVGE MEKRYRLMSK MGVRNLAGYN
     TKIRDAIKRE EPIPNPFSLT PDQPEPLSPL PTIVVVIDEL ADLMMVVGKK IEELIARLAQ
     KARAAGIHLI LATQRPSVDV ITGLIKANIP TRIAFQVSSK IDSRTILDQM GAETLLGQGD
     MLYMPPGTGL PVRVHGAFCS DDEVHRVVES LKAQGEPNYV EGLLEGGLDG DGAEGASSVT
     GIGGDAESDP MYDQACEVVL KHRRASISLV QRHLRIGYNR AARLLEQMEQ SGMVSAMQSN
     GNREILVPAA AAREEA
//
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