ID A0A1D8G7G7_9ACTN Unreviewed; 964 AA.
AC A0A1D8G7G7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=DNA translocase SpoIIIE {ECO:0000313|EMBL:AOT61380.1};
GN Name=spoIIIE {ECO:0000313|EMBL:AOT61380.1};
GN ORFNames=A4G23_04267 {ECO:0000313|EMBL:AOT61380.1};
OS Streptomyces rubrolavendulae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=285473 {ECO:0000313|EMBL:AOT61380.1, ECO:0000313|Proteomes:UP000095349};
RN [1] {ECO:0000313|EMBL:AOT61380.1, ECO:0000313|Proteomes:UP000095349}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJM4426 {ECO:0000313|EMBL:AOT61380.1,
RC ECO:0000313|Proteomes:UP000095349};
RA Kim J.-G.;
RT "Streptomyces rubrolavendulae MJM4426 Genome sequencing and assembly.";
RL Submitted (SEP-2016) 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; CP017316; AOT61380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1D8G7G7; -.
DR STRING; 285473.A4G23_04267; -.
DR KEGG; srn:A4G23_04267; -.
DR PATRIC; fig|285473.5.peg.4480; -.
DR Proteomes; UP000095349; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000095349};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 134..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..216
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 253..277
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 611..811
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 331..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..464
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 628..635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 964 AA; 101229 MW; 5E997BA4E45E8786 CRC64;
MSSAPRTGNL TPMASRTSGK GPHGTAGTAK PRAAGRTTGA AQKAAPGKPP ARKTAAKQPA
PARKGAAKKA PAKKTAKKAA ARTAPKPAPS PTGGVYRIVR ALWLGLAHAV GALFRGIGRG
AKGLDPAHRK DGLALLLLGL ALVVAAGTWA NLQGPVGDLV DMLVTGAFGR LDLLVPLLIG
TMAVRLILHP EKPEANGRIV IGLSALAIGV LGQVHIACGS PGRDEGAQAM QDAGGLIGWA
ASTPLIFMTG EVLTVPLLVL LTVFGLLVVT ATPVNAIPRR LRALGERLGV LEPYETWTED
DQRYDEQWRE GLPASARRRS GAPAAPGADG YDPDRAEDEA LTRRRRTRTR KAADAADPAF
GRPLDPVDIA AAAAADLDGA VLNGMPPSPL VADLTRDVTP DRAPEPTGGA TAAAGSGGAG
RAAGRGRGGA GAPAVPPARE EGDGRVPDLT KPAPVREEPE PMPARAEQLR LAGDITYALP
SLDLLERGGP GKTRSAANDA IVASLRNVFS EFKVDADVTG FTRGPTVTRY EVELGPAVKV
ERITALTKNI AYAVASPDVR IISPIPGKSA VGIEIPNTDR EMVNLGDVLR LADAAEDDHP
MLVALGKDVE GGYVMANLAK MPHVLVAGAT GSGKSSCINC LITSVMIRAT PEDVRMVLVD
PKRVELTAYE GIPHLITPII TNPKRAAEAL QWVVREMDLR YDDLAAFGYR HIDDFNAAVR
SGKLTTPPGS ERELQPYPYL LVIVDELADL MMVAPRDVED AIVRITQLAR AAGIHLVLAT
QRPSVDVVTG LIKANVPSRL AFATSSLADS RVILDQPGAE KLIGKGDGLF LPMGANKPVR
LQGAFVTEDE VAAVVRHCKE QMEPVFRDDV TTGTKQKKEI DEEIGDDLDL LCQAAELVVS
TQFGSTSMLQ RKLRVGFAKA GRLMDLMESR NIVGPSEGSK ARDVLVKPDD LDGVLALIRG
ESGS
//
