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Database: UniProt
Entry: A0A0U3MDB3_9BURK
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Original site: A0A0U3MDB3_9BURK 
ID   A0A0U3MDB3_9BURK        Unreviewed;       420 AA.
AC   A0A0U3MDB3;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Transcription termination factor Rho {ECO:0000256|HAMAP-Rule:MF_01884};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01884};
DE   AltName: Full=ATP-dependent helicase Rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   Name=rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   ORFNames=DES44_2095 {ECO:0000313|EMBL:REG19597.1}, RD2015_2147
GN   {ECO:0000313|EMBL:ALV06621.1};
OS   Roseateles depolymerans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Roseateles.
OX   NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV06621.1, ECO:0000313|Proteomes:UP000060699};
RN   [1] {ECO:0000313|EMBL:ALV06621.1, ECO:0000313|Proteomes:UP000060699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV06621.1,
RC   ECO:0000313|Proteomes:UP000060699};
RA   Kim K.M.;
RT   "Complete genome of Roseateles depolymerans KCTC 42856.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:REG19597.1, ECO:0000313|Proteomes:UP000256283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11813 {ECO:0000313|EMBL:REG19597.1,
RC   ECO:0000313|Proteomes:UP000256283};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-2018) 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:0000256|HAMAP-Rule:MF_01884}.
CC   -!- SUBUNIT: Homohexamer. The homohexamer assembles into an open ring
CC       structure. {ECO:0000256|HAMAP-Rule:MF_01884}.
CC   -!- SIMILARITY: Belongs to the Rho family. {ECO:0000256|HAMAP-
CC       Rule:MF_01884, ECO:0000256|PROSITE-ProRule:PRU01203}.
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DR   EMBL; CP013729; ALV06621.1; -; Genomic_DNA.
DR   EMBL; QUMT01000002; REG19597.1; -; Genomic_DNA.
DR   RefSeq; WP_058934867.1; NZ_QUMT01000002.1.
DR   AlphaFoldDB; A0A0U3MDB3; -.
DR   STRING; 76731.RD2015_2147; -.
DR   KEGG; rdp:RD2015_2147; -.
DR   PATRIC; fig|76731.3.peg.2198; -.
DR   OrthoDB; 9805197at2; -.
DR   Proteomes; UP000060699; Chromosome.
DR   Proteomes; UP000256283; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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: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_C; 1.
DR   Gene3D; 1.10.720.10; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00767; rho; 1.
DR   PANTHER; PTHR46425; TRANSCRIPTION TERMINATION FACTOR RHO; 1.
DR   PANTHER; PTHR46425:SF1; TRANSCRIPTION TERMINATION FACTOR RHO; 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; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF68912; Rho N-terminal domain-like; 1.
DR   PROSITE; PS51856; RHO_RNA_BD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01884};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01884};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01884}; Reference proteome {ECO:0000313|Proteomes:UP000060699};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW   ECO:0000256|HAMAP-Rule:MF_01884}.
FT   DOMAIN          48..123
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000259|PROSITE:PS51856"
FT   REGION          61..66
FT                   /note="RNA-binding 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   REGION          78..80
FT                   /note="RNA-binding 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   REGION          108..110
FT                   /note="RNA-binding 1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   REGION          284..288
FT                   /note="RNA-binding 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         169..174
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         181..186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         212
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   SITE            326
FT                   /note="RNA-binding 2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ   SEQUENCE   420 AA;  47556 MW;  136F7535BB8910C4 CRC64;
     MHLSELKALH VSALIKMGEE LEIDNVARLR KQELMFAIMK KRAKAGEQVF GDGVLEVLPD
     GFGFLRSPET SYMASTDDIY LSPSQIRRFN LHTGDMIEGE VRVPKDGERY FALVKVDRVN
     GLTPEESKHK IMFENLTPLF PKEQFKLERD IRGDDNITSR IIDLIAPLGK GQRALLVAPP
     KSGKTVMMQH LAHSIAANYP DAHLMVLLVD ERPEEVTEMQ RTVRGEVISS TFDEPAARHV
     QVAEMVIERA KRLVELRKDV IILLDSITRL ARAYNNVLPS SGKVLTGGVD ANALQRPKRF
     FGAARNIEEG GSLTIIGTAL VDTGSKMDEV IYEEFKGTGN CEIHLDRRMA EKRVYPSILL
     NKSGTRREEL LLKPEILQKA WILRKLLYPM DEIEAMEFIL DKMKSSKNNH DFFDMMRRGG
//
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