RHO_STRM9
ID RHO_STRM9 Reviewed; 416 AA.
AC D1AWS1;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 19-JAN-2010, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Smon_0262;
OS Streptobacillus moniliformis (strain ATCC 14647 / DSM 12112 / NCTC 10651 /
OS 9901).
OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Streptobacillus.
OX NCBI_TaxID=519441;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14647 / DSM 12112 / NCTC 10651 / 9901;
RX DOI=10.4056/sigs.48727;
RA Nolan M., Gronow S., Lapidus A., Ivanova N., Copeland A., Lucas S.,
RA Glavina Del Rio T., Chen F., Tice H., Pitluck S., Cheng J.F., Sims D.,
RA Meincke L., Bruce D., Goodwin L., Brettin T., Han C., Detter J.C., Pati A.,
RA Mavromatis K., Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Rohde M., Sproer C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Streptobacillus moniliformis type strain
RT (9901T).";
RL Stand. Genomic Sci. 1:300-307(2009).
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; CP001779; ACZ00747.1; -; Genomic_DNA.
DR RefSeq; WP_012858304.1; NC_013515.1.
DR AlphaFoldDB; D1AWS1; -.
DR SMR; D1AWS1; -.
DR STRING; 519441.Smon_0262; -.
DR PRIDE; D1AWS1; -.
DR EnsemblBacteria; ACZ00747; ACZ00747; Smon_0262.
DR GeneID; 29674055; -.
DR KEGG; smf:Smon_0262; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_0; -.
DR OMA; TRLCRAH; -.
DR OrthoDB; 1619125at2; -.
DR Proteomes; UP000002072; 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 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; 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; 1.
DR Pfam; PF00006; ATP-synt_ab; 1.
DR Pfam; PF07497; Rho_RNA_bind; 1.
DR SMART; SM00382; AAA; 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..416
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000398672"
FT DOMAIN 51..121
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT BINDING 162..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 174..179
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 416 AA; 46939 MW; EA727678AAE43C06 CRC64;
MENITLDELG NFTLTNLRKL AKEHKIEGYS TIPKMELLNR LCYSIATAEG LIYSYGELDI
INETYGFLRN TPQNIDVYVS NSQIKKFGLR QGDVIVGEVR KPLNDEKNFG LLKLIYVNGE
KGELSRQRPI FDDLTPSYPI ERLELGEGTV SSRIIDLIAP IGKGQRGLIV APPKAGKTTI
LSDLANDILK YNKDVQVWII LIDERPEEVT DIKENVKNAE IFAATFDENT SVHLSVTEKV
LEAAKREIEK GNNIVILMDS LTRLARSYNI EMPSSGKLLS GGIDPKSLYM PKKFLGAARK
IRGGGSLTIL ATALIETGSR MDEVIFEEFK GTGNMELVLD RALQQLRLFP AVDILKSGTR
KEELLYSKRE FDSILKLRKF LLKLNEAEAL KFLMDLIKRY SSNKDLLENI DYELKL