RHO_THEMA
ID RHO_THEMA Reviewed; 427 AA.
AC P38527;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 147.
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=TM_1470;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-427.
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 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS), AND SUBUNIT.
RX PubMed=20452362; DOI=10.1016/j.jmb.2010.05.004;
RA Canals A., Uson I., Coll M.;
RT "The structure of RNA-free Rho termination factor indicates a dynamic
RT mechanism of transcript capture.";
RL J. Mol. Biol. 400:16-23(2010).
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 ECO:0000269|PubMed:20452362}.
CC -!- SIMILARITY: Belongs to the Rho family. {ECO:0000255|HAMAP-
CC Rule:MF_01884}.
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DR EMBL; L27279; AAA59210.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36538.1; -; Genomic_DNA.
DR PIR; G72246; G72246.
DR RefSeq; NP_229270.1; NC_000853.1.
DR RefSeq; WP_004081775.1; NZ_CP011107.1.
DR PDB; 3L0O; X-ray; 2.35 A; A/B=1-427.
DR PDBsum; 3L0O; -.
DR AlphaFoldDB; P38527; -.
DR SMR; P38527; -.
DR STRING; 243274.THEMA_06950; -.
DR EnsemblBacteria; AAD36538; AAD36538; TM_1470.
DR KEGG; tma:TM1470; -.
DR eggNOG; COG1158; Bacteria.
DR InParanoid; P38527; -.
DR OMA; TRLCRAH; -.
DR OrthoDB; 1619125at2; -.
DR EvolutionaryTrace; P38527; -.
DR Proteomes; UP000008183; 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 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; RNA-binding; Transcription; Transcription regulation;
KW Transcription termination.
FT CHAIN 1..427
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188980"
FT DOMAIN 55..130
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"
FT HELIX 10..15
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 18..27
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 33..35
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 38..47
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 51..64
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 75..77
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 90..95
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 103..109
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 117..126
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 161..169
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 188..202
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 206..212
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 229..233
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 240..259
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 263..269
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 290..292
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 299..306
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 331..338
FT /evidence="ECO:0007829|PDB:3L0O"
FT TURN 339..341
FT /evidence="ECO:0007829|PDB:3L0O"
FT STRAND 344..349
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 351..354
FT /evidence="ECO:0007829|PDB:3L0O"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 372..374
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 378..391
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 396..408
FT /evidence="ECO:0007829|PDB:3L0O"
FT HELIX 413..419
FT /evidence="ECO:0007829|PDB:3L0O"
SQ SEQUENCE 427 AA; 48302 MW; 37748653910AFC95 CRC64;
MSEEQKTISI SELESMNIKQ LYEIAKSLGI PRYTSMRKRD LIFAILKAQT ESTGYFFGEG
VLEIHPEGFG FLRRIEDNLL PSNDDIYISP SQIRKFNLNT GDIISGVIRK PKEGEKYFAM
IKIEAINYRP VEAVNDRVNF DNLTPDYPRE RFILETDPKI YSTRLIDLFA PIGKGQRGMI
VAPPKAGKTT ILKEIANGIA ENHPDTIRII LLIDERPEEV TDIRESTNAI VIAAPFDMPP
DKQVKVAELT LEMAKRLVEF NYDVVILLDS LTRLARVYNI VVPPSGKLLT GGVDPAALYK
PKRFFGAARN TREGGSLTII ATALVETGSK MDEVIFEEFK GTGNMELVLS RQLANKRIFP
AINLLLSGTR REELLLDEET LKKVWLLRRM LSAMTEEEGL TLILNKLSET SSNEEFLKLI
DKEKARY
