RHO_MICLU
ID RHO_MICLU Reviewed; 691 AA.
AC P52154;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 107.
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};
OS Micrococcus luteus (Micrococcus lysodeikticus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX NCBI_TaxID=1270;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-6 AND 290-298.
RC STRAIN=EM;
RX PubMed=8557681; DOI=10.1074/jbc.271.2.742;
RA Nowatzke W.L., Richardson J.P.;
RT "Characterization of an unusual Rho factor from the high G + C Gram-
RT positive bacterium Micrococcus luteus.";
RL J. Biol. Chem. 271:742-747(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 206-691.
RC STRAIN=EM;
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 [3]
RP SEQUENCE REVISION TO 501.
RA Nowatzke W.L.;
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
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; L27277; AAB18671.1; -; Genomic_DNA.
DR AlphaFoldDB; P52154; -.
DR SMR; P52154; -.
DR PRIDE; P52154; -.
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; 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; 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 TIGRFAMs; TIGR00767; rho; 1.
DR PROSITE; PS51856; RHO_RNA_BD; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Helicase; Hydrolase;
KW Nucleotide-binding; RNA-binding; Transcription; Transcription regulation;
KW Transcription termination.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8557681"
FT CHAIN 2..691
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188968"
FT DOMAIN 307..390
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 48..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..277
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 433..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 445..450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT CONFLICT 292
FT /note="G -> P (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 691 AA; 75162 MW; 8B3DD0F444D577E6 CRC64;
MTESTEQTTP TNGGGLASLK LAQLQALASQ LGIAGGSRMR KADLVTAISD HQRGGSVADR
DAAERAAQAP AAPAAETAPA AASSEDAAPA AERPARRRSR RADADTSAPA AAQDGQPQAE
AREAQTEQAP RETASDQDRS GGSEARDEGE DRPQSERRSR GRRRAGDDDA QQGQDRRSDG
AQGEDGADAD RRGDREDRDD NGRENGRGRN GRNGRDRDNG RDRENGRENS RDRENGRDGS
REQRGDKSED GGRGDGGRGD RSRRDDRDDE GGRNRRNRRN RNERGRNRRG RGGPEVDETE
LTEDDVLQPV AGILDVLDNY AFVRTSGYLP GPNDVYVSLA MVKKYGLRKG DAVVGPIAPR
DGEKQQHHGG GSNRQKFNAL VKISSVNGQP AVEHPQRVEF GKLVPLYPQE RLRLETDPKL
IGPRVIDLVS PIGKGQRGLI VSPPKAGKTM ILQSIANAIK TNNPEVHLMM VLVDERPEEV
TDMQRSVDGE VIASTFDRPA DDHTTLAELA IERAKRLVEM GRDVVVLLDS MTRLGRAYNL
AAPASGRILS GGVDSSALYP PKKFFGAARN IENGGSLTIL ATALVETGSR MDEVIFEEFK
GTGNMELRLS RHLAERRIFP AVDVNASGTR REEALLSQEE VKIMWKLRRV LSGLEQQQAL
DLLTNKIKDT ASNAEFLMLV SKTTLGSKGD D
