ID A0A1B9EWN5_9ACTN Unreviewed; 941 AA.
AC A0A1B9EWN5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=DNA translocase SpoIIIE {ECO:0000313|EMBL:OCC12098.1};
GN Name=spoIIIE {ECO:0000313|EMBL:OCC12098.1};
GN ORFNames=A3Q37_02289 {ECO:0000313|EMBL:OCC12098.1};
OS Streptomyces sp. PTY087I2.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1819298 {ECO:0000313|EMBL:OCC12098.1, ECO:0000313|Proteomes:UP000093256};
RN [1] {ECO:0000313|EMBL:OCC12098.1, ECO:0000313|Proteomes:UP000093256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTY087I2 {ECO:0000313|EMBL:OCC12098.1,
RC ECO:0000313|Proteomes:UP000093256};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-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}.
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:OCC12098.1}.
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DR EMBL; LZRD01000008; OCC12098.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1B9EWN5; -.
DR PATRIC; fig|1819298.4.peg.2384; -.
DR Proteomes; UP000093256; Unassembled WGS sequence.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000093256}.
FT DOMAIN 588..788
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 305..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 393..426
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; 100021 MW; 4E5716646755C532 CRC64;
MFTGDDSGNL GIMASRTSGK GSQGTAGTAK RVGRTPGPAK KAAPAKKTAP KKSAAPAKKA
PAKKAAAKKP APKPAPSPTG GVYRLVRAVW LGMAHGVGAV FRSIGRGAKG LDPAHRKDGL
ALLLLGLALI VAAGTWSHLQ GPVGDLVEML VTGAFGRLDL LAPILLGAMA VRLILYPERP
EANGRIVIGL SALVIGVLGQ VHIACGTPGR DAGTEAMQDA GGLVGWAASK PLIFMMGEVL
AVPLLVLLTV FGLLVVTATP VNAIPQRLRQ LGVRLGIVEP LPEAHEGYED DDERYEEQWR
EALPERTRRR GTRRTDADPV YDHDQAEAEA LSKRRRTRKP SAQPAMNRPL DAVDVAAAAA
AALDGAVLNG MPPSPVVADL TQGVSVDRER TGTPVPGARE AEREERPKPG VRRSAPEPEG
AEERSGGVPD LTKPAPESSP GLPARAEQLQ LSGDITYSLP SLDLLERGGP GKTRSAANDR
VVESLTTVFT EFKVDAAVTG FTRGPTVTRY EVELGPAVKV EKITALTKNI AYAVASPDVR
IISPIPGKSA VGIEIPNSDR EMVNLGDVLR LAEDDDPMMV AFGKDVEGGY VMHSLAKMPH
MLVAGATGSG KSSCINCLIT SIMVRATPED VRMVLVDPKR VELTAYEGIP HLITPIITNP
KKAAEALQWV VREMDLRYDD LAAFGYRHID DFNKAVREGK VKLPEGSERE LSPYPYLLVI
VDELADLMMV APRDVEDSIV RITQLARAAG IHLVLATQRP SVDVVTGLIK ANVPSRLAFA
TSSLADSRVI LDQPGAEKLI GKGDGLFLPM GANKPTRMQG AFVTEDEVAA VVQHCKDQMA
PVFRDDVVVG TKQKKEIDED IGDDLDLLCQ AAELVVSTQF GSTSMLQRKL RVGFAKAGRL
MDLMESRSIV GPSEGSKARD VLVKPDELDG VLAVIRGESA P
//
