ID H0R1Y9_9ACTN Unreviewed; 1003 AA.
AC H0R1Y9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:GAB19094.1};
GN Name=ftsK {ECO:0000313|EMBL:GAB19094.1};
GN ORFNames=GOEFS_075_00140 {ECO:0000313|EMBL:GAB19094.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB19094.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB19094.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB19094.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) 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. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination.
CC {ECO:0000256|ARBA:ARBA00024986}.
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:GAB19094.1}.
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DR EMBL; BAEH01000075; GAB19094.1; -; Genomic_DNA.
DR AlphaFoldDB; H0R1Y9; -.
DR STRING; 1077974.GOEFS_075_00140; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000035034; 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:GAB19094.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000035034};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 186..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 644..844
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 346..522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..368
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 485..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 661..668
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1003 AA; 106160 MW; EEAB03A6051373A9 CRC64;
MASKATARAG ARSSAGGTRG SSARGTSGTR SAGGSQRGGA RKSTATNAAK SKAPAKSTSK
GSSTKTAPRK SAAKTRSGSA TRSASAGRVS TASADIHHRR PSVAASAGRG LGAGWTLLAR
GVGSLARMGA GSTRGGDDRY DYDEIPFDED ENEFLDQPAP RDSHSGMRRV PAGADGHSHR
RDGAGLALIV VAAVIGAGVW FAAAGPAGAF IDTLVRAIVG VVAVVVPIAL VALGIMLMRR
PPNPRRRPHY IGAGLLIGLP LLGLIHLIAG SPRGLDARSD AGGYLGFVVG TPLTNAVTEW
ISVPIFLLCM AFGGLLLSGR TVREVVDAIA GYLGLSHDDQ YYDDDYYDDG EYDDYDDEAP
DVDEAEDDHE FGAAPAAERS ADPYDNYPPD EQPARRRRSR KAAPTSAGAA DILADLTTEP
IGGIRRTPVS PDMVTEPISD DTDDLFADPA PTSRSTPKRK TAGEAARERA AQESARSAPK
PVVAPVIEDR DDDADNEPLA RPMADSEGTY RLPPPSLLID GDPPKLGSSA NDEMIERIGT
VLEQFKIDAA VTGYTRGPTV TRYEVELGPG VKVEKITALQ RNIAYAAATD NVRLLAPIPG
KSAVGIEVPN ADREMVRLAD VLASPKNRKD RHPLVIGLGK DIEGDFVTAN LAKMPHLLVA
GSTGSGKSSF VNSMLVSLLQ RATPDEVRMI LIDPKMVELT PYEGIPHLIT PIITQPKKAA
AALAWLVEEM EQRYQDMKSS RVRHIDDFNA KVASGEISTP LGSERVYKPY PYILAIVDEL
ADLMMTAPRD VEDAIVRITQ KARAAGIHLV LATQRPSVDV VTGLIKTNVP SRLAFATSSL
TDSRVILDQP GAEKLIGMGD GLFLPMGANK PIRMQGAFIT DEEISAVVDY TREQAEPEYT
EGVTAAKASD KKDIDADIGN DLDDLLQAIE LVVSSQFGST SMLQRKLRVG FAKAGRLMDL
METRGVVGPS EGSKAREVLV KPEDLAGVIT SITGGGAEDD STE
//
