ID V6KPN4_STRRC Unreviewed; 935 AA.
AC V6KPN4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:EST34150.1};
GN ORFNames=M878_11495 {ECO:0000313|EMBL:EST34150.1};
OS Streptomyces roseochromogenus subsp. oscitans DS 12.976.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1352936 {ECO:0000313|EMBL:EST34150.1, ECO:0000313|Proteomes:UP000017984};
RN [1] {ECO:0000313|EMBL:EST34150.1, ECO:0000313|Proteomes:UP000017984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS 12.976 {ECO:0000313|EMBL:EST34150.1,
RC ECO:0000313|Proteomes:UP000017984};
RX PubMed=24407645;
RA Ruckert C., Kalinowski J., Heide L., Apel A.K.;
RT "Draft Genome Sequence of Streptomyces roseochromogenes subsp. oscitans DS
RT 12.976, Producer of the Aminocoumarin Antibiotic Clorobiocin.";
RL Genome Announc. 2:e01147-e01113(2014).
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 -!- 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:EST34150.1}.
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DR EMBL; AWQX01000089; EST34150.1; -; Genomic_DNA.
DR AlphaFoldDB; V6KPN4; -.
DR STRING; 1352936.M878_11495; -.
DR PATRIC; fig|1352936.5.peg.2438; -.
DR HOGENOM; CLU_001981_2_2_11; -.
DR Proteomes; UP000017984; Chromosome.
DR GO; GO:0016020; C: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: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; 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; 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:0000313|EMBL:EST34150.1};
KW Cell division {ECO:0000313|EMBL:EST34150.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000017984};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 235..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 582..782
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 14..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 385..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..61
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 935 AA; 99559 MW; 4ED8D9EF0E673795 CRC64;
MKLWAHVSAV VSPGNLTPMA SRPSAAKKQT AKKAAAPAKA PAKKAAAKKA AAKKAPAKRA
PAKKAAPKPA PSPTGGVYRL VRALWLGLAH AVGAVFRGIG KGAKNLDPAH RKDGIALLLF
GIALIVAAGT WANLKGPVGD LVEILVTGAF GRLDLLVPIL LAVIAVRFIR HPEQPEANGR
IVIGLSALVI GVLGQVHIAC GSPARGDGMQ AIRDAGGLIG WAAATPLTYA MTEVLAVPLL
VLLTIFGLLV VTATPVNAIP QRLRALGVRL GVLHDHDTDG YEGYEEYTDD DARYDEQWRE
ALPARSRKRS SAPKAYDPDS VEEEALSQRR GRPRRSAVPQ PDPQRQMDAV DVAAAAAAAL
DGAVLHGMPP SPLVADLTQG VSIGDREETT PVPTPAPASQ PSPVPAARPK QEKLQPGTVP
DLTKKAPAEP RDLPPRAEQL QLSGDITYAL PSLDLLTRGG PGKARSEAND AVVASLTQVF
TEFKVDAAVT GFTRGPTVTR YEVELGPAVK VERITALTKN IAYAVASPDV RIISPIPGKS
AVGIEIPNTD REMVNLGDVL RLAESAEDDD PMLVAFGKDV EGGYVMHSLA KMPHMLVAGA
TGSGKSSCIN CLITSVMMRA TPEDVRLILV DPKRVELTAY EGIPHLITPI ITNPKRAAEA
LQWVVREMDL RYDDLAAYGY RHIDDFNQAV REGKVKPPEG SERELQPYPY LLVIVDELAD
LMMVAPRDVE DSIVRITQLA RAAGIHLVLA TQRPSVDVVT GLIKANVPSR LAFATSSLAD
SRVILDQPGA EKLIGKGDGL FLPMGANKPT RMQGAFVTEA EVAAVVRHCK DQMTPVFRDD
VTVGTKQKKE IDEDIGDDLD LLCQAAELVV STQFGSTSML QRKLRVGFAK AGRLMDLMES
RGIVGPSEGS KARDVLVKPD ELDGVLALIR GESEE
//
