RHO_STRLI
ID RHO_STRLI Reviewed; 707 AA.
AC P52157;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 98.
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};
OS Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RC STRAIN=ZX7;
RX PubMed=8702978; DOI=10.1074/jbc.271.36.21803;
RA Ingham C.J., Hunter I.S., Smith M.C.M.;
RT "Isolation and sequencing of the rho gene from Streptomyces lividans ZX7
RT and characterization of the RNA-dependent NTPase activity of the
RT overexpressed protein.";
RL J. Biol. Chem. 271:21803-21807(1996).
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.
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 -!- CAUTION: It is uncertain whether Met-1 or Met-43 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA64720.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X95444; CAA64719.1; -; Genomic_DNA.
DR EMBL; X95444; CAA64720.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; P52157; -.
DR SMR; P52157; -.
DR PRIDE; P52157; -.
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 ATP-binding; Helicase; Hydrolase; Nucleotide-binding; RNA-binding;
KW Transcription; Transcription regulation; Transcription termination.
FT CHAIN 1..707
FT /note="Transcription termination factor Rho"
FT /id="PRO_0000188979"
FT DOMAIN 331..406
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 76..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..284
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 449..454
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 461..466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT BINDING 492
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ SEQUENCE 707 AA; 76544 MW; 012B5F85C623E616 CRC64;
MSDTTDLMGA RVEETAAAPA TDASAPATGA GSRRRRGTGL EGMVLAELQQ VASGLGIRGT
ARMRKSQLIE VIKEAQAAGG APAKAAPAAA DTAGETKPKR RSTSRTRTGD EAPAEKAEKA
GKADKKADKA AADKAAAQQQ IEIPGQPTPK VNASAEQAAP ADDAPSERRR RRATSDAGSP
SATDTTVAVE TRAEPKADTS APQQSQGHQQ GQGDARSDAE GGDGRRRDRR DRGDRDRGDR
GDRGDRGDRG DRGERGRDRR NKGDDQQNQG GGRQDRQQQG GGGRQDRQQH DDGYDDDGSG
RRGRRGRYRD RRGRRGRDEI QEPQINEDDV LIPVAGILDI LDNYAFIRTS GYLPGPNDVY
VSLAQVRKNG LRKGDHLTGA VRQPKEGERR EKFNALVRLD SVNGMAPEHG RGRPEFNKLT
PLYPQDRLRL ETDPGVLTTR IIDLVAPIGK GQRGLIVAPP KTGKTMIMQA IANAITHNNP
ECHLMVVLVD ERPEEVTDMQ RSVKGEVISS TFDRPAEDHT TVAELAIERA KRLVELGHDV
VVLLDSITRL GRAYNLAAPA SGRILSGGVD STALYPPKRF FGAARNIEDG GSLTILATAL
VDTGSRMDEV IFEEFKGTGN AELKLDRKLA DKRIFPAVDV DASGTRKEEI LLGSDELAIT
WKLRRVLHAL DQQQAIELLL DKMKQTKSNA EFLIQIQKTT PTPGNGD
