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Database: UniProt
Entry: A0A0Q4RYQ0_9BURK
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ID   A0A0Q4RYQ0_9BURK        Unreviewed;       779 AA.
AC   A0A0Q4RYQ0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KQO27620.1};
GN   ORFNames=ASF16_01935 {ECO:0000313|EMBL:KQO27620.1};
OS   Acidovorax sp. Leaf78.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1736237 {ECO:0000313|EMBL:KQO27620.1, ECO:0000313|Proteomes:UP000051234};
RN   [1] {ECO:0000313|Proteomes:UP000051234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA   Garrido-Oter R., Mueller D.B.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000051234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf78 {ECO:0000313|Proteomes:UP000051234};
RA   Vorholt J.;
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:KQO27620.1}.
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DR   EMBL; LMLZ01000001; KQO27620.1; -; Genomic_DNA.
DR   RefSeq; WP_056161876.1; NZ_LMLZ01000001.1.
DR   AlphaFoldDB; A0A0Q4RYQ0; -.
DR   STRING; 1736237.ASF16_01935; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000051234; 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: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, ECO:0000313|EMBL:KQO27620.1};
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        29..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        82..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          423..632
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          698..717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         440..447
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   779 AA;  84649 MW;  5EC89896617C6E1B CRC64;
     MTYSLNTLNA SSAAKSPPRT GAARFGHEIG LMLGLLALVF WLLALVSYSA QDAAFSNSGA
     RDVRMVANWA GRFGAWLADG SYFALGFSVW WCVAAGVRAW LSSLARWMRG GEQVPGAATP
     MQRRALFWVG LVVLLCASTA LEWSRLYRFE ALLPGGHAGG VLGYVTGPAS VKWLGYTGSA
     LLSIVLAVLG AALVFRFSWG HVAEVLGSRI DTLVQSRLAK REVAKDVAVG RKAARERAVV
     VLEERTESEV HHPEPIQIIE PILVDVPQST RVVKERQKPL FTEMPDSKLP LVDLLDGPQQ
     RQETVAPETL EMTSRLIEKK LKDFGVEVRV VAAMPGPVIT RYEIEPATGV KGSQIVGLAK
     DLARSLSLVS IRVVETIPGK NFMALELPNA KRQSIRLSEI LGSQVYHEAK SMLTMGLGKD
     IVGNPVVADL AKMPHVLVAG TTGSGKSVGI NAMILSLLYK AEARDVRLLM IDPKMLEMSV
     YEGIPHLLAP VVTDMKQAAH GLNWCVAEME RRYKLMSKLG VRNLAGYNVK IDEAKAREEF
     IYNPFSLTPE EPEPLQRLPH IVVIIDELAD LMMVVGKKIE ELIARLAQKA RAAGIHLILA
     TQRPSVDVIT GLIKANIPTR IAFSVGSKID SRTILDQMGA EALLGMGDML YMASGTGLPI
     RVHGAFVSDE EVHRVVSYLK QQGEPDYIDG VLEGGTVDGE GDLSGEGGSG DGGEKDPMYD
     QAVEVVLKDR KASISYVQRK LRIGYNRSAR LLEDMEKAGL VSGLTASGQR EVLVPNRSE
//
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