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Database: UniProt
Entry: G8N1Z3_GEOTH
LinkDB: G8N1Z3_GEOTH
Original site: G8N1Z3_GEOTH 
ID   G8N1Z3_GEOTH            Unreviewed;       751 AA.
AC   G8N1Z3;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   SubName: Full=DNA segregation ATPase FtsK/SpoIIIE {ECO:0000313|EMBL:AEV18788.1};
GN   ORFNames=GTCCBUS3UF5_14750 {ECO:0000313|EMBL:AEV18788.1};
OS   Geobacillus thermoleovorans CCB_US3_UF5.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1111068 {ECO:0000313|EMBL:AEV18788.1, ECO:0000313|Proteomes:UP000005636};
RN   [1] {ECO:0000313|EMBL:AEV18788.1, ECO:0000313|Proteomes:UP000005636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCB_US3_UF5 {ECO:0000313|EMBL:AEV18788.1,
RC   ECO:0000313|Proteomes:UP000005636};
RA   Muhd Sakaff M.K.L., Abdul Rahman A.Y., Saito J.A., Hou S., Alam M.;
RT   "Complete genome sequence of thermophilic Geobacillus thermoleovorans
RT   CCB_US3_UF5.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; CP003125; AEV18788.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8N1Z3; -.
DR   KEGG; gte:GTCCBUS3UF5_14750; -.
DR   PATRIC; fig|1111068.3.peg.1428; -.
DR   HOGENOM; CLU_001981_9_6_9; -.
DR   Proteomes; UP000005636; 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:0007059; P:chromosome segregation; 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}; Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        30..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        141..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          415..611
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          192..231
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          244..275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..262
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         432..439
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   751 AA;  82499 MW;  F64AA387966617C6 CRC64;
     MIGLGLLAVA VVAMARLGLV GETLVLVGRF FFGEWYMLLV GGLFLLSLIV MWRREWPSWT
     GRPFVGASSI AAALLLLSHD KLFELMSRRG ELDPSIIRTT WGLFWNEASG KAADVDLGGG
     MVGALLFAAS YQLFDSPGTK WICFLLFIVG FVVLTGKSLR ETAGKWVAFA AAFVRKEWLA
     FVEDIKQWRA GRKRKESGGR SRRSRRAAAK REDEPAEASS VEPDEELLSP PPIISDFAAV
     RSAAEPEEEK NPLVEGDSGG EEDKPAPPLA FSEHENTNYD LPPLDLLRLP KPAGQSADHA
     NIYANARKLE KTFQSFGVKA KVTQVHLGPA VTKYEVYPDV GVKVSKIVSL SDDLALALAA
     KDIRIEAPIP GKSAIGIEVP NEEIATVSLR EVLEAIEHTR DKAKLLIPLG RDISGEVVAA
     ELNKMPHLLI AGATGSGKSV CINGIIVSLL MRTKPHEVKL MMIDPKMVEL SVYNGVPHLL
     TPVVTDAKKA AQALKKVVQE MERRYELFSH TGTRNIEGYN EHIRHHNETA SEQQPLLPYI
     VVIIDELADL MMVASSDVEE AITRLAQMAR AAGIHLIIAT QRPSVDVITG VIKANIPSRI
     AFSVSSQIDS RTILDMGGAE KLLGRGDMLF LPMGASKPVR VQGAFVSDQE VEEVVRFVIG
     QQQAQYYEEM FVEDSEPSSS ALEDELYDEA VRLVVEMQSA SVSMLQRRFR IGYNRAARLI
     DAMEERGVVG PYEGSKPRAV LWSKEDLKKT S
//
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