ID D9W129_9ACTN Unreviewed; 941 AA.
AC D9W129;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=DNA translocase ftsK {ECO:0000313|EMBL:EFL18005.1};
GN ORFNames=SSNG_05257 {ECO:0000313|EMBL:EFL18005.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL18005.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL18005.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL18005.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) 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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; GG657750; EFL18005.1; -; Genomic_DNA.
DR RefSeq; WP_007266931.1; NZ_GG657750.1.
DR AlphaFoldDB; D9W129; -.
DR STRING; 253839.SSNG_05257; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_2_1_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
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 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}; 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 101..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..156
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..246
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 588..788
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 264..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 605..612
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 941 AA; 98449 MW; 27515DD955D5A2EC CRC64;
MASSTSGKGS QSTAGAAKGR TGRTTAPTKK AAPRKPPAKK AAAAKRPAAK KAAAKPAPSP
SGGVVRLVRW CWLGLAHAVG GLFRGIGRGA RNLDPAHRKD GVALLLLALA LIVAAGTWSN
LSGPVGELVT MLVTGAFGRL DLLVPILLGV MAARFIRHPE QTDANGRIGI GLSALVIGVL
GLVHIACGAP GRDEGTTAMQ NAGGLIGWAA SKPLIFTMGA PLAVPMLVLL TVFGLLVVTA
TPVAAIPQRL RRAGIRLGVI QPNEYDEGYG EPHEGAGRPG RPDRHDAEQW QARAGGAGGA
GGAVDEAEEA ALARRRRPRR SAARPGGREP DAVDVAAAAA AALDGVVYGG LPPNPLVADL
TQGIAGRGEG AEITAPVPPA REERPAAARA PAPVQAPAPA DGPDGRDDAD GAPHERTAAV
SGTLSVPDLT KTPPPAQPLP ARAEQLQLRG DITYALPSLE LLEKGGPGKT RSAANDTVVA
ALTNVFTEFK VDAQVTGFTR GPTVTRYEVT LGAAVKVERI TALAKNIAYA VASPDVRIIS
PIPGKSAVGI EIPNTDREMV NLGDVLRLAD AAEDDHPMLV ALGKDVEGGY VMANLAKMPH
VLVAGATGSG KSSCINCLIT SIMVRATPED VRMVLVDPKR VELTAYEGIP HLITPIITNP
KRAAEALQWV VREMDLRYDD LAAFGYRHID DFNQAIRDGK IKLPPGSERE LSPYPYLLVI
VDELADLMMV APRDVEDSIV RITQLARAAG IHLVLATQRP SVDVVTGLIK ANVPSRLAFA
TSSLADSRVI LDQPGAEKLI GKGDGLFLPM GANKPVRLQG AFVTEEEIAG IVQHCKDQMT
PVFRDDVTVG QKQKKEIDEE IGDDLDLLCQ AAELVVSTQF GSTSMLQRKL RVGFAKAGRL
MDLMESRGVV GPSEGSKARD VLVKPDELDG VLAVIRGEEA P
//
