RHO_BUCBP
ID RHO_BUCBP Reviewed; 419 AA.
AC Q89A22;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Transcription termination factor Rho {ECO:0000255|HAMAP-Rule:MF_01884};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01884};
DE AltName: Full=ATP-dependent helicase Rho {ECO:0000255|HAMAP-Rule:MF_01884};
GN Name=rho {ECO:0000255|HAMAP-Rule:MF_01884}; OrderedLocusNames=bbp_538;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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:0000255|HAMAP-Rule:MF_01884}.
CC -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC structure. {ECO:0000255|HAMAP-Rule:MF_01884}.
CC -!- SIMILARITY: Belongs to the Rho family. {ECO:0000255|HAMAP-
CC Rule:MF_01884}.
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DR EMBL; AE016826; AAO27237.1; -; Genomic_DNA.
DR RefSeq; WP_011091638.1; NC_004545.1.
DR AlphaFoldDB; Q89A22; -.
DR SMR; Q89A22; -.
DR STRING; 224915.bbp_538; -.
DR PRIDE; Q89A22; -.
DR EnsemblBacteria; AAO27237; AAO27237; bbp_538.
DR GeneID; 56471072; -.
DR KEGG; bab:bbp_538; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_6; -.
DR OMA; TRLCRAH; -.
DR OrthoDB; 1619125at2; -.
DR Proteomes; UP000000601; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 1.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR46425; PTHR46425; 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; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF68912; SSF68912; 1.
DR TIGRFAMs; TIGR00767; rho; 1.
DR PROSITE; PS51856; RHO_RNA_BD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..419
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188959"
FT DOMAIN 48..123
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 61..66
FT /note="RNA-binding 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT REGION 78..80
FT /note="RNA-binding 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT REGION 108..110
FT /note="RNA-binding 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT REGION 284..288
FT /note="RNA-binding 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 169..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 181..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 212
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT SITE 326
FT /note="RNA-binding 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 419 AA; 46971 MW; CFD3F8C2B1D7D4A2 CRC64;
MNLTALKNIP VSELIFLGDN AGLENLARMR KQDIIFSILK QHAKSGEDIF GDGVLEILQD
GFGFLRSSDS SYLAGPDDIY VSPSQIRRFN LRTGDTISGK IRPPKEGERY FALLKVNKVN
YDKPENARSK ILFENLTPLH ANSRLRMERG NGSTEDLTAR VLDLASPIGR GQRGLIVAPP
KAGKTMLLQN IAQSIAYNHP DCVLMVLLID ERPEEVTEMR RLVKGEVVAS TFDEPSSRHV
QVSEMVIEKA KRLVEHKKDV IILLDSITRL ARAYNTVVPA SGKVLTGGVD ANALHRPKRF
FGAARNVEEG GSLTIIATAL IDTGSKMDEV IYEEFKGTGN MELPLSRKIA EKRVFPAIDY
NRSGTRKEEL LTKSDELQKM WILRKIIHPM SEIDAMEFLI NKLAMTKTNN EFFDMMKRS
