ID RHO_DEIRA Reviewed; 426 AA.
AC P52153;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 27-MAR-2024, entry version 142.
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=DR_1338;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=298;
RX PubMed=8051015; DOI=10.1128/jb.176.16.5033-5043.1994;
RA Opperman T., Richardson J.P.;
RT "Phylogenetic analysis of sequences from diverse bacteria with homology to
RT the Escherichia coli rho gene.";
RL J. Bacteriol. 176:5033-5043(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; L27276; AAA59208.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF10910.1; -; Genomic_DNA.
DR PIR; H75407; H75407.
DR RefSeq; NP_295061.1; NC_001263.1.
DR AlphaFoldDB; P52153; -.
DR SMR; P52153; -.
DR STRING; 243230.DR_1338; -.
DR PaxDb; 243230-DR_1338; -.
DR EnsemblBacteria; AAF10910; AAF10910; DR_1338.
DR KEGG; dra:DR_1338; -.
DR PATRIC; fig|243230.17.peg.1535; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_0; -.
DR InParanoid; P52153; -.
DR OrthoDB; 9805197at2; -.
DR Proteomes; UP000002524; Chromosome I.
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; 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; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW RNA-binding; Transcription; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..426
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188961"
FT DOMAIN 58..131
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT BINDING 176..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 188..193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 219
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT CONFLICT 1..8
FT /note="MTVTEVAP -> MTATDAA (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="A -> G (in Ref. 1; AAA59208)"
FT /evidence="ECO:0000305"
FT CONFLICT 93
FT /note="V -> I (in Ref. 1; AAA59208)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="Q -> L (in Ref. 1; AAA59208)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="S -> T (in Ref. 1; AAA59208)"
FT /evidence="ECO:0000305"
FT CONFLICT 203
FT /note="T -> V (in Ref. 1; AAA59208)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="A -> S (in Ref. 1; AAA59208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 426 AA; 47131 MW; 249E4EAC6FAF62A3 CRC64;
MTVTEVAPQA LPFQELQEKI LPELHLLAAG LGIENYRKLK KDALALAIME KQADAEGQSL
ARGYLDITSD GYGFLQADLL DPASRSVLVT AGVIKQYHLR TGDEVIGRAR KPRENERYGS
LVRVEAVNGL DPEAARQRPR FDDLTPTFPD QQLVLEDPST DDGLSLRVVD LLVPIGRGQR
ALIVAPPKAG KTTLLKKIAN SITKNYPDVT VMVLLVDERP EEVTDFRESV QGAQVIASTF
DEPPQHHVRV AEFVHERARR IVEEGGHVVI LLDSITRLAR ANNLVTPPTG RTLSGGLDSN
ALHWPKRFLG AARNIREGGS LTILATALVE TGSRMDDVIF EEFKGTGNAE LVLSRRLEER
RIFPALDILK SGTRREELLL QPEVLKKMWL LRKVISDMDP ADAMEMLLGR MGKTRNNVEF
LAALAG
//
