RHO_FIBSS
ID RHO_FIBSS Reviewed; 689 AA.
AC C9RLJ9; D9S7L5;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 1.
DT 03-AUG-2022, entry version 82.
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};
GN OrderedLocusNames=Fisuc_2428, FSU_2991;
OS Fibrobacter succinogenes (strain ATCC 19169 / S85).
OC Bacteria; Fibrobacteres; Fibrobacterales; Fibrobacteraceae; Fibrobacter.
OX NCBI_TaxID=59374;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Weimer P.J.,
RA Stevenson D.M., Boyum J., Brumm P.I., Mead D.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19169 / S85;
RA Durkin A.S., Nelson K.E., Morrison M., Forsberg C.W., Wilson D.B.,
RA Russell J.B., Cann I.K.O., Mackie R.I., White B.A.;
RT "Complete sequence of Fibrobacter succinogenes subsp. succinogenes S85.";
RL Submitted (AUG-2010) 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ADL26535.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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; CP001792; ACX76014.1; -; Genomic_DNA.
DR EMBL; CP002158; ADL26535.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; C9RLJ9; -.
DR SMR; C9RLJ9; -.
DR STRING; 59374.Fisuc_2428; -.
DR PRIDE; C9RLJ9; -.
DR EnsemblBacteria; ADL26535; ADL26535; FSU_2991.
DR KEGG; fsc:FSU_2991; -.
DR KEGG; fsu:Fisuc_2428; -.
DR PATRIC; fig|59374.8.peg.2862; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_0; -.
DR Proteomes; UP000000517; Chromosome.
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 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; IPR011113; Rho_RNA-bd.
DR InterPro; IPR004665; Term_rho.
DR PANTHER; PTHR46425; PTHR46425; 2.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF07497; Rho_RNA_bind; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00357; CSP; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
DR SUPFAM; SSF52540; SSF52540; 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..689
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000398668"
FT DOMAIN 287..362
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 63..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 405..410
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 417..422
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 448
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 689 AA; 78252 MW; A29E2230CAFEC603 CRC64;
MPRTPKNQNL EQNTQTQSLT DLVYPESTGI PVPEYLGTVD KLPDNTEEVP QPKRRGRKPN
PKTKARKEPA LEQNVQAETE PEFQEKKQPV DGIAAAEKRL AEQYGVANID AIAEPIYTGE
QNYKPAESTE ENAFVSENTS EAVIPQNGDM AQAQAENQGE VATDQNADPN AQQQGEAQAQ
NGEGQDDRRF NNQNGKFNKF NKNNKFNKNN RNNRNFQQQE EFVDDSATLP APGSEAILKA
KENWLKFRKL SMSELQELAV QKEVDFRRMR KQSLNYILQS LENEGNIIYT EGVLEVTPQG
HGFLRMPDQN YQTSADDVYV SQNLIRKFNL KIGDTIEGLV RTPRDQDKYF SMRRIDRVNF
EEPDKMRRRV AFEYLTPIHP EEKIHLEWNE TEYSTRIMDL FSPIGKGQRS IILAPPRTGK
TVLLQNVTRA IAKNHPEIIL ITLLIDERPE EVTEMRDIIT DIKEKAAEKG IEIKAEVVAS
TFDEPPEHHT RVANMVLEKA KRLVESQKDV VILLDSITRF ARANNVVIPH SGKILSGGVD
ANAMQFPKKF FGAARKIQDK IRTVKNEDGT ISEEVQKNGS LTIIGTALIE TGSRMDEVIF
EEFKGTGNME LVLDRRIAEK RIWPAIDVFK SGTRKEERLL TLLEQNAAWN FRRGSQNETE
TGIMENLLKL MSKLKTNAEL LAVLSKPKV
