ID A0A1J4PU59_9ACTN Unreviewed; 941 AA.
AC A0A1J4PU59;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:OIK24453.1};
GN ORFNames=VT52_027105 {ECO:0000313|EMBL:OIK24453.1};
OS Streptomyces malaysiense.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428626 {ECO:0000313|EMBL:OIK24453.1, ECO:0000313|Proteomes:UP000034838};
RN [1] {ECO:0000313|Proteomes:UP000034838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA Lee L.H., Chan K.-G.;
RT "Genome sequencing of Streptomyces sp. MUSC136T.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OIK24453.1, ECO:0000313|Proteomes:UP000034838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC136T {ECO:0000313|Proteomes:UP000034838};
RA Lee L.-H., Ser H.-L.;
RT "Genome sequence of Streptomyces malaysiense MUSC 136.";
RL Submitted (OCT-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:OIK24453.1}.
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DR EMBL; LBDA02000068; OIK24453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4PU59; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000034838; 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 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:OIK24453.1};
KW Cell division {ECO:0000313|EMBL:OIK24453.1};
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:UP000034838};
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 588..788
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..61
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..343
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; 100103 MW; 5DEDD317163B4A9E CRC64;
MSVVVSPGNL TPMASRPSAA KKQPAKKAAA PAKGPAKKAV AAKKAPARKA PAKKAPARKA
AVKKAPPRPA PSPTGGVYRL ARALWLGLAH AVGAVFRGIG QGARNLDPAH RKDGVALLLF
GIALIVAAGT WADLKGPVGD LVEILVTGAF GRLDLLVPIL LAVIAVRLIR HPEKPEANGR
IVIGLSALLV GVLGQVHIAC GSPARSDGMQ AIRDAGGLIG WAAATPLTYT MTEMLAVPLL
VLLTVFGLLV VTATPVNAIP QRLRALGVRL GVLHEHEPEE FGEDDERYEE QWREALPARS
RVRSGGSRSY DPDEAEEEAL SSRRGRPRRS AVPQPDPRRR MDAVDVAAAA AAALDGAVQH
GLPPSPLVAD LTQGVSVGDR EETTPVPAPD APAAADPEPA PAKAARPSAR PVPAARPERG
GGSVVPDLTK QTPEEPRELP ARAEQLQLSG DITYSLPALD LLQRGGPGKV RSEANDAIVA
SLTQVFTEFK VDAAVTGFTR GPTVTRYEVE LGPAVKVERI TALTKNIAYA VASPDVRIIS
PIPGKSAVGI EIPNTDREMV NLGDVLRLAE SAEDDDPMLV AFGKDVEGGY VMHSLAKMPH
MLVAGATGSG KSSCINCLIT SIMMRATPED VRMILVDPKR VELTAYEGIP HLITPIITNP
KRAAEALQWV VREMDLRYDD LAAYGYRHID DFNRAVREGR AKPPEGSERE LQPYPYLLVI
VDELADLMMV APRDVEDSIV RITQLARAAG IHLVLATQRP SVDVVTGLIK ANVPSRLAFA
TSSLADSRVI LDQPGAEKLI GKGDGLFLPM GANKPTRMQG AFVTEEEVAE VVRHCKEQMA
PVFREDVTVG TKQKKEIDED IGDDLDLLCQ AAELVVSTQF GSTSMLQRKL RVGFAKAGRL
MDLMESRGIV GPSEGSKARD VLVKPDDLDG VLAVIRGESE G
//
