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Database: UniProt
Entry: A0A0T2YYR3_9BURK
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Original site: A0A0T2YYR3_9BURK 
ID   A0A0T2YYR3_9BURK        Unreviewed;       782 AA.
AC   A0A0T2YYR3;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KRC04097.1};
GN   ORFNames=ASE11_03260 {ECO:0000313|EMBL:KRC04097.1};
OS   Hydrogenophaga sp. Root209.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1736490 {ECO:0000313|EMBL:KRC04097.1, ECO:0000313|Proteomes:UP000050889};
RN   [1] {ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|Proteomes:UP000050889};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC04097.1, ECO:0000313|Proteomes:UP000050889}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root209 {ECO:0000313|EMBL:KRC04097.1,
RC   ECO:0000313|Proteomes:UP000050889};
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   -!- 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:KRC04097.1}.
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DR   EMBL; LMIE01000012; KRC04097.1; -; Genomic_DNA.
DR   RefSeq; WP_056269531.1; NZ_LMIE01000012.1.
DR   AlphaFoldDB; A0A0T2YYR3; -.
DR   STRING; 1736490.ASE11_03260; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000050889; 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: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; 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; 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:KRC04097.1};
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        27..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        128..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          424..633
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         441..448
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   782 AA;  85474 MW;  B78F15D9A2BBB0D0 CRC64;
     MTYSLNTLNA DRADQPQVGV SRFAQEIGLV LGAAALAFWL LALLSHSLAD PAWSTTGTAT
     EVGNWGGRLG ALLADWSYYL FGFSVWWCFL VGVRAWLSAL AGWIRGTRDE DGDGPDPRIW
     HRPWARRTLF WLALVTLMAA STVLEWSRLY RLEALLPGHA GGVLGHGLGA FSVRWLGFTG
     SALAMLALLL VCLPRVFRFS WGHWAEEVGH TLDGWFEARR EKREAVEDQR IGEKAARERE
     EVVKVERVEI EEHHPTPVVI EPTLVDVPKS ERVAKERQKP LFTELPDSKL PQVDLLDSAP
     VHQAGVDSQT LEMTSRLIEK KLKDFGVDVR VVAAAPGPVI TRYEIEPATG VKGSQIVNLG
     RDLARSLSLV SIRVIETIPG KNLMALELPN AKRQTIKLSE ILGSQVYNDA KSMLTMGLGK
     DIGGQPIVAD LAKMPHCLVA GTTGSGKSVG INAMILSLLY KADARDVRLL LIDPKMLEMS
     VYEGIPHLLA PVVTDMKHAA NGLNWCVAEM EKRYKLMSKL GVRNLAGYNV KIDEAAARGE
     FIGNPFSLTP EQPEPLERLP YIVVVIDELA DLMMVVGKKI EELIARLAQK ARAAGIHLIL
     ATQRPSVDVI TGLIKANIPT RLSFQVSSKI DSRTILDQMG AESLLGMGDM LYMPSGTGFP
     IRVHGAFVSD DEVHRVVAYL KEQGGEPNYI DGVLEGGVTD GEGGDLFGEG GGEGSGEKDA
     LYDQAVEIVI KDRKASISYV QRKLKIGYNR AARLLEDMEN AGLVSALTSS GQRDILVPAR
     GE
//
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