GenomeNet

Database: UniProt
Entry: H5SDJ7_9BACT
LinkDB: H5SDJ7_9BACT
Original site: H5SDJ7_9BACT 
ID   H5SDJ7_9BACT            Unreviewed;       420 AA.
AC   H5SDJ7;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Transcription termination factor Rho {ECO:0000256|HAMAP-Rule:MF_01884};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01884};
DE   AltName: Full=ATP-dependent helicase Rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   Name=rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   ORFNames=HGMM_F13G06C16 {ECO:0000313|EMBL:BAL54233.1};
OS   uncultured Acetothermia bacterium.
OC   Bacteria; Candidatus Bipolaricaulota; environmental samples.
OX   NCBI_TaxID=236499 {ECO:0000313|EMBL:BAL54233.1};
RN   [1] {ECO:0000313|EMBL:BAL54233.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16309394; DOI=10.1111/j.1462-2920.2005.00881.x;
RA   Nunoura T., Hirayama H., Takami H., Oida H., Nishi S., Shimamura S.,
RA   Suzuki Y., Inagaki F., Takai K., Nealson K.H., Horikoshi K.;
RT   "Genetic and functional properties of uncultivated thermophilic
RT   crenarchaeotes from a subsurface gold mine as revealed by analysis of
RT   genome fragments.";
RL   Environ. Microbiol. 7:1967-1984(2005).
RN   [2] {ECO:0000313|EMBL:BAL54233.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Takami H., Noguchi H., Takaki Y., Uchiyama I., Toyoda A., Nishi S.,
RA   Chee G.-J., Arai W., Nunoura T., Itoh T., Hattori M., Takai K.;
RT   "A Deeply Branching Thermophilic Bacterium with an Ancient Acetyl-CoA
RT   Pathway Dominates a Subsurface Ecosystem.";
RL   PLoS ONE 7:e30559-e30559(2012).
CC   -!- FUNCTION: Facilitates transcription termination by a mechanism that
CC       involves Rho binding to the nascent RNA, activation of Rho's RNA-
CC       dependent ATPase activity, and release of the mRNA from the DNA
CC       template. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC   -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC       structure. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC   -!- SIMILARITY: Belongs to the Rho family. {ECO:0000256|HAMAP-
CC       Rule:MF_01884, ECO:0000256|PROSITE-ProRule:PRU01203}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP011682; BAL54233.1; -; Genomic_DNA.
DR   AlphaFoldDB; H5SDJ7; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008186; F:ATP-dependent activity, acting on RNA; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR   CDD; cd04459; Rho_CSD; 1.
DR   CDD; cd01128; rho_factor_C; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   HAMAP; MF_01884; Rho; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd.
DR   InterPro; IPR011129; CSD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041703; Rho_factor_ATP-bd.
DR   InterPro; IPR011112; Rho_N.
DR   InterPro; IPR036269; Rho_N_sf.
DR   InterPro; IPR011113; Rho_RNA-bd.
DR   InterPro; IPR004665; Term_rho.
DR   NCBIfam; TIGR00767; rho; 1.
DR   PANTHER; PTHR46425; TRANSCRIPTION TERMINATION FACTOR RHO; 1.
DR   PANTHER; PTHR46425:SF1; TRANSCRIPTION TERMINATION FACTOR RHO; 1.
DR   Pfam; PF00006; ATP-synt_ab; 1.
DR   Pfam; PF07498; Rho_N; 1.
DR   Pfam; PF07497; Rho_RNA_bind; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00357; CSP; 1.
DR   SMART; SM00959; Rho_N; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF68912; Rho N-terminal domain-like; 1.
DR   PROSITE; PS51856; RHO_RNA_BD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01884};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01884};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW   ECO:0000256|HAMAP-Rule:MF_01884}.
FT   DOMAIN          52..125
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000259|PROSITE:PS51856"
FT   BINDING         168..173
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         180..185
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         211
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ   SEQUENCE   420 AA;  47146 MW;  9E056A64164BA69D CRC64;
     MGDLLDITEL KSKDMSELRA LAEQFGINGR GRIKKEDLVF AILKAQAEKQ GLHFKDGVLE
     ILPDGYGFLR DSSCLPGAHD IYVSPSQIKR FALKDGDVVS GIVRPPKEDE KYFALLKIEA
     INFEDPEAIR NRQAFEDLIP YHPREQLKLE YDSNEFSTRI IDLFAPIGKG QRGLIVSPPK
     AGKTTLLKHI AHGIAANHPE VYLIVLLVDE RPEEVTDFRE SITMGEVVAA TFDQKPEIHC
     RISELVIAKA KRLVEMGRDV VILMDSITRL ARAYNLAIAP SGKLLSGGMD PTALYKPKEF
     LGAARNIKDG GSLTIIGTAL IDTGSRLDQV VFEEFKGTGN MELVLDRNLA NKRIFPAIDL
     EASGTRKEEL LLPEKVLKRV WVLRKLIGDM NDKQKALEWI LSRMEQTKTN EQFLELMRNE
//
DBGET integrated database retrieval system