RHO_GEMAT
ID RHO_GEMAT Reviewed; 737 AA.
AC C1A5H8;
DT 05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 67.
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=GAU_0446;
OS Gemmatimonas aurantiaca (strain T-27 / DSM 14586 / JCM 11422 / NBRC
OS 100505).
OC Bacteria; Gemmatimonadetes; Gemmatimonadales; Gemmatimonadaceae;
OC Gemmatimonas.
OX NCBI_TaxID=379066;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-27 / DSM 14586 / JCM 11422 / NBRC 100505;
RA Takasaki K., Ichikawa N., Miura H., Matsushita S., Watanabe Y., Oguchi A.,
RA Ankai A., Yashiro I., Takahashi M., Terui Y., Fukui S., Yokoyama H.,
RA Tanikawa S., Hanada S., Kamagata Y., Fujita N.;
RT "Complete genome sequence of Gemmatimonas aurantiaca T-27 that represents a
RT novel phylum Gemmatimonadetes.";
RL Submitted (MAR-2006) 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; AP009153; BAH37488.1; -; Genomic_DNA.
DR AlphaFoldDB; C1A5H8; -.
DR SMR; C1A5H8; -.
DR STRING; 379066.GAU_0446; -.
DR EnsemblBacteria; BAH37488; BAH37488; GAU_0446.
DR KEGG; gau:GAU_0446; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_3_0_0; -.
DR OMA; TTDLMGA; -.
DR Proteomes; UP000002209; 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; SSF52540; SSF52540; 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..737
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000398670"
FT DOMAIN 367..439
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 1..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 349..363
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 487..492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 499..504
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 530
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 737 AA; 81379 MW; A87328EE12F28151 CRC64;
MSGPCSAHRV PPIGPRPTIR SPRITRSSRM TEPKRPSRRG TTRTRPAPDS VGDDNPYLDA
PASRASSESR SESGSGLSAE GSGSDAPRPR RPRQPRRPAA DAESAPTAAD TNDSAPAPTA
RRGVRRTTRS AAAGTDVSSS TSELPRAESP RSEPRTESRP EPRAENGSET RHESRGGSSE
GRPSFRDPSP SGYEASMERP LADRPDAPNR YDRAFDRTDG PERQDTRPER PFQQERPFQQ
DRQDRHERQD RPDRRDRNGR RRGRGGRPDN RGPGGDRHQS TGPAADRSHD RGPDRNNERA
FDRPERPDRQ GESSDRFDSQ DRGGNRQRNG RRGRNRFRRG AGGNESAPIS GSHAPSQGSP
SAPIGVEGTM AGWFDPSRDG GFLRRPENSY LPDPTDPFMP PALVRLHQLR RGDRLEVTYG
RDHRGRYLVI EVQTLNDGSP VVLEKRPDFN TLVASYPDRK LTLETGRPAK TGPELTRRAI
DLIAPIGYGQ RALIVAPARA GKTTLLQAIV EGVSINHPEA VLLVLLVDER PEEVSEMITW
GYGEVVASSF DMPPKRHVEV AEMTLERARR LVEQGKDVVI VLDSITRLAR AHNTVDRGTG
RTMSGGLDAT AMQKPKAFFG SARMIAPQHG GGSLTIIATA LVETGSRMDD VIFEEFKGTG
NCEIKLDRSL ADRRIFPAFD IATSGTRREE KLYRPDQLEK VHLLRRGLHQ LPPQAGMEWL
IKRIAATTNN DSLLDGL
