ID   RHO_SULMS               Reviewed;         379 AA.
AC   C7LJY3;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-OCT-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=SMDSEM_012;
OS   Sulcia muelleri (strain SMDSEM).
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Candidatus Sulcia.
OX   NCBI_TaxID=595499;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMDSEM;
RX   PubMed=19706397; DOI=10.1073/pnas.0906424106;
RA   McCutcheon J.P., McDonald B.R., Moran N.A.;
RT   "Convergent evolution of metabolic roles in bacterial co-symbionts of
RT   insects.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15394-15399(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; CP001605; ACU52745.1; -; Genomic_DNA.
DR   AlphaFoldDB; C7LJY3; -.
DR   SMR; C7LJY3; -.
DR   STRING; 595499.SMDSEM_012; -.
DR   PRIDE; C7LJY3; -.
DR   EnsemblBacteria; ACU52745; ACU52745; SMDSEM_012.
DR   KEGG; sms:SMDSEM_012; -.
DR   HOGENOM; CLU_016377_4_3_10; -.
DR   OMA; NTIAYNH; -.
DR   Proteomes; UP000008074; 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; 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; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR041703; Rho_factor_ATP-bd.
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; RNA-binding;
KW   Transcription; Transcription regulation; Transcription termination.
FT   CHAIN           1..379
FT                   /note="Transcription termination factor Rho"
FT                   /id="PRO_0000398675"
FT   DOMAIN          1..68
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT   BINDING         111..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT   BINDING         123..128
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT   BINDING         154
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ   SEQUENCE   379 AA;  43128 MW;  170C2ECEEE6007BC CRC64;
     MTDKYGFLRS SYTNYLSSSK DVYVSQSQIR LFRIKTGDTI RGEVRTPNPK KGEKYFPLKR
     IFQINGRFPT SVIKRKSFKK LTPLFPNEKF QISKRKVTLS TRIVDFFSPL GKGQRGIIVA
     PPKTGKTTLL KEIANTIAYN HPEVYLIILL IDERPEEVTD MQRNVNGEVV YSTFDEPAEK
     HVKVANIVLQ KAKRMVECGH DVVILLDSIT RLARAYNTVS PTSGKILSGG VDSNALQKPK
     RFFGAARNIE YGGSLSIIAT AIIETGSKMD EVIFEEFKGT GNMELQLDRK IANKRIFPAI
     DLNASSTRKE EFLLTKYNLN KMFLIRKLLA EMTSVEAIDF IKTRLMKTKN NQEFFKSIKS
     SIKSSIKSSR DRENIEKKI