RHO_CERS4
ID RHO_CERS4 Reviewed; 422 AA.
AC P52156; Q3IYH2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, 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=RHOS4_28440;
GN ORFNames=RSP_1231;
OS Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=272943;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8606169; DOI=10.1128/jb.178.7.1946-1954.1996;
RA Gomelsky M., Kaplan S.;
RT "The Rhodobacter sphaeroides 2.4.1 rho gene: expression and genetic
RT analysis of structure and function.";
RL J. Bacteriol. 178:1946-1954(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC / NCIMB 8253 / ATH 2.4.1.;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL Submitted (SEP-2005) 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; L76097; AAB02034.1; -; Genomic_DNA.
DR EMBL; CP000143; ABA80412.1; -; Genomic_DNA.
DR PIR; JC6035; JC6035.
DR RefSeq; WP_009563271.1; NZ_CP030271.1.
DR RefSeq; YP_354313.1; NC_007493.2.
DR AlphaFoldDB; P52156; -.
DR SMR; P52156; -.
DR STRING; 272943.RSP_1231; -.
DR EnsemblBacteria; ABA80412; ABA80412; RSP_1231.
DR GeneID; 57471562; -.
DR GeneID; 67448003; -.
DR KEGG; rsp:RSP_1231; -.
DR PATRIC; fig|272943.9.peg.3212; -.
DR eggNOG; COG1158; Bacteria.
DR OMA; TRLCRAH; -.
DR PhylomeDB; P52156; -.
DR Proteomes; UP000002703; Chromosome 1.
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..422
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188974"
FT DOMAIN 52..127
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT BINDING 173..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 185..190
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 422 AA; 47238 MW; 8D116C7BD98BE274 CRC64;
MNERLNLADL KAKTPADLLA MAEEWEIENA PSMRKGEMMF SILKEHAEEG YEVGGDGVLE
VLQDGFGFLR SPEANYLPGP DDIYVSPEIL RQFSLRTGDT IEGVIVAPRE NERYFSLTRV
TKINFDDPER ARHKVHFDNL TPLYPDERLK MEVDDPTMKD RSARIIDLVA PIGKGQRGLI
VAPPRTGKTV LLQNIAHSIA TNHPECYLIV LLIDERPEEV TDMQRSVKGE VVSSTFDEPA
TRHVAVAEMV IEKAKRLVEH KRDVVILLDS ITRLGRAFNT VVPSSGKVLT GGVDANALQR
PKRFFGAARN IEEGGSLTII ATALIDTGSR MDEVIFEEFK GTGNSEIVLD RKVADKRVFP
AMDILKSGTR KEDLLVDKSD LQKTYVLRRI LNPMGTTDAI EFLISKLRQT KSNAEFFDSM
NT
