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Database: UniProt
Entry: A0A095BA67_9SPHN
LinkDB: A0A095BA67_9SPHN
Original site: A0A095BA67_9SPHN 
ID   A0A095BA67_9SPHN        Unreviewed;       770 AA.
AC   A0A095BA67;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=FG95_00145 {ECO:0000313|EMBL:KGB59237.1};
OS   Sphingopyxis sp. LC363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1120705 {ECO:0000313|EMBL:KGB59237.1, ECO:0000313|Proteomes:UP000029625};
RN   [1] {ECO:0000313|EMBL:KGB59237.1, ECO:0000313|Proteomes:UP000029625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC363 {ECO:0000313|EMBL:KGB59237.1,
RC   ECO:0000313|Proteomes:UP000029625};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (MAY-2014) 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:KGB59237.1}.
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DR   EMBL; JNFC01000001; KGB59237.1; -; Genomic_DNA.
DR   RefSeq; WP_037553265.1; NZ_JNFC01000001.1.
DR   AlphaFoldDB; A0A095BA67; -.
DR   STRING; 1120705.FG95_00145; -.
DR   PATRIC; fig|1120705.3.peg.146; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000029625; 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   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};
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}; Reference proteome {ECO:0000313|Proteomes:UP000029625};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        21..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        112..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          405..624
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          211..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          746..770
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         422..429
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   770 AA;  82904 MW;  670FF819BB910C57 CRC64;
     MASRKAAPAK ADWRTVFRQS VARSLVIAAA VALGLFTLFL TLALITYDST DAALNTAAHG
     TAANWMGSAG AWFADLGLSI GGVGVALLLP LLGIIAWRLW TGEAQPYWPR QLAYSFIGIL
     FVGLGAELWS PATNAPLPAG WGGIIALLLG GAIAPLFAQA GEPAAALIRF ATILLLVGLG
     LWLAWRALRL EKGWASRFRL PAATSSRIAE PVRAPRADDR VPGPLESAVR PRAVAEPVDR
     APPEIADPAQ RSAPSKPRPK PQTELFTNYQ LPSIDLLAPA PDRPAGQIDK AALERNARLL
     ESVLEDFQVK GVVTAVRPGP VVTMYELEPA PGTKASRVSN LADDIARNMS ALSARIAPIP
     GRTVIGIELP NAQREAVVLH EIIGSALFQD QTGALPIILG KNISGDAMIA DLAPMPHLLI
     AGTTGSGKSV GLNAMILSLL YRLGPDQVKM IMIDPKMLEL SVYDDIPHLL APVVTEPKKA
     IRALKWAVEQ MEDRYRMMSS LSVRNLASYN DKVRGALAKG KSLGRRVQTG YDPDTGQPVY
     EEETLDYQPL PQIVVVVDEL ADLMMTAGKE VEFLIQRLAQ KARAAGIHLI LATQRPSVDV
     ITGVIKANLP TRISFNVTSK IDSRTILGEA GAEQLLGKGD MLYVPGGKQI TRIHGPFVSD
     DEVRLVAEHW KAQGRPDYIE SVTEDPEDGG FAMEGAPAGG DSAEDRMYAK ACQIVAESQK
     ASTSWLQRQL RIGYNSAARL IERMEEEGIV SPPNHVGRRD VLTDQYGQPR
//
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