ID A0A0A7PPV3_9SPHN Unreviewed; 770 AA.
AC A0A0A7PPV3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN Name=ftsK {ECO:0000313|EMBL:AJA11263.1};
GN ORFNames=SKP52_22060 {ECO:0000313|EMBL:AJA11263.1};
OS Sphingopyxis fribergensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1515612 {ECO:0000313|EMBL:AJA11263.1, ECO:0000313|Proteomes:UP000030907};
RN [1] {ECO:0000313|EMBL:AJA11263.1, ECO:0000313|Proteomes:UP000030907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Kp5.2 {ECO:0000313|EMBL:AJA11263.1,
RC ECO:0000313|Proteomes:UP000030907};
RX PubMed=26040579; DOI=10.1099/ijs.0.000371;
RA Oelschlagel M., Ruckert C., Kalinowski J., Schmidt G., Schlomann M.,
RA Tischler D.;
RT "Description of Sphingopyxis fribergensis sp. nov. - a soil bacterium with
RT the ability to degrade styrene and phenylacetic acid.";
RL Int. J. Syst. Evol. Microbiol. 65:3008-3015(2015).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP009122; AJA11263.1; -; Genomic_DNA.
DR RefSeq; WP_039578737.1; NZ_CP009122.1.
DR AlphaFoldDB; A0A0A7PPV3; -.
DR STRING; 1515612.SKP52_22060; -.
DR KEGG; sphk:SKP52_22060; -.
DR HOGENOM; CLU_001981_6_2_5; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000030907; Chromosome.
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};
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 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 231..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..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; 83051 MW; A5FFD42570C8F4DE CRC64;
MASRKAAPAK ADWRTVFRQS IARSLVIAAA VALGFFTLFL TLALVTYDST DAALNTAAHG
TAANWMGSAG AWFADLGLSI GGAGIVLLLP LLGIMAWRLW TGEAQPYWPR QLAYCFIGIL
LVGLGAELWS PATNAPMPAG WGGIIALLIG GAVAPLFAQA GEPAAALIRF ATILLLVLFG
LWLAWRALRL EKGWASRFKL PAAEGSRIVE PARVPNDETK APNLMERVVR PRAVAEPSDR
APPEIAEPAE RSAPSKPRPK PQTELFTNYQ LPSIDLLAPP PPGPTGQIDK AGLERNARLL
ESVLEDFQVK GVVTAVRPGP VVTMYELEPA PGTKASRVSN LADDIARNMS ALSARIAPIP
GRTVIGIELP NAVRESVVLH EIIGSALFQD QTGALPIILG KNISGDPMIA DLAPMPHLLI
AGTTGSGKSV GLNAMILSLL YRLGPDQVKM IMIDPKMLEL SVYDDIPHLL APVVTEPKKA
IRALKWAVEQ MEDRYRMMSS LSVRNLASYN DKVRGALAKG KSLGRRVQTG YDPDTGQPVY
EEETLDYAPL PQIVVVVDEL ADLMMTAGKE VEFLIQRLAQ KARAAGIHLI LATQRPSVDV
ITGVIKANLP TRISFNVTSK IDSRTILGEA GAEQLLGKGD MLYVPGGKQI TRIHGPFVSD
DEVRAVADHW KGQGRPDYIE SVTEDPEDGG FAMEGAPAGG DSAEDRMYAK ACQIVVESQK
ASTSWLQRQL RIGYNSAARL IERMEEEGLV SPPNHVGRRD VLTDQYGQQR
//
