ID   RHO_BORBU               Reviewed;         515 AA.
AC   P33561; O51248;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 3.
DT   03-AUG-2022, entry version 143.
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=BB_0230;
OS   Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS   (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=224326;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8451174; DOI=10.1093/nar/21.4.1040;
RA   Tilly K., Campbell J.;
RT   "A Borrelia burgdorferi homolog of the Escherichia coli rho gene.";
RL   Nucleic Acids Res. 21:1040-1040(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX   PubMed=9403685; DOI=10.1038/37551;
RA   Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA   Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA   Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA   Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA   van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA   Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA   Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA   Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL   Nature 390:580-586(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 142-331.
RC   STRAIN=212;
RX   PubMed=7812434; DOI=10.1099/13500872-140-11-2931;
RA   Ojaimi C., Davidson B.E., Saint-Girons I., Old I.G.;
RT   "Conservation of gene arrangement and an unusual organization of rRNA genes
RT   in the linear chromosomes of the Lyme disease spirochaetes Borrelia
RT   burgdorferi, B. garinii and B. afzelii.";
RL   Microbiology 140:2931-2940(1994).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA71920.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; L07656; AAA71920.1; ALT_INIT; Unassigned_DNA.
DR   EMBL; U35673; AAB41463.1; -; Genomic_DNA.
DR   EMBL; AE000783; AAC66619.1; -; Genomic_DNA.
DR   EMBL; L46347; AAA73991.1; -; Genomic_DNA.
DR   PIR; F70128; F70128.
DR   RefSeq; NP_212364.1; NC_001318.1.
DR   RefSeq; WP_010889711.1; NC_001318.1.
DR   AlphaFoldDB; P33561; -.
DR   SMR; P33561; -.
DR   STRING; 224326.BB_0230; -.
DR   PRIDE; P33561; -.
DR   EnsemblBacteria; AAC66619; AAC66619; BB_0230.
DR   KEGG; bbu:BB_0230; -.
DR   PATRIC; fig|224326.49.peg.629; -.
DR   HOGENOM; CLU_016377_4_3_12; -.
DR   OMA; TRLCRAH; -.
DR   Proteomes; UP000001807; 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; 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; 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   SMART; SM00357; CSP; 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..515
FT                   /note="Transcription termination factor Rho"
FT                   /id="PRO_0000188956"
FT   DOMAIN          146..221
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT   BINDING         264..269
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT   BINDING         276..281
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT   BINDING         307
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT   CONFLICT        154
FT                   /note="D -> H (in Ref. 3; AAA73991)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="E -> D (in Ref. 3; AAA73991)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   515 AA;  57625 MW;  7F6FD5C41C7D7671 CRC64;
     MDKKNGGFDL ESEIRRLDVS KEFKIEDNLK KKVVKVVAKK DSASSVTKSA DLSGVKDSNG
     VIFSDFDYDI PSSGLENNIK TLEQSNIIKF FNGKDYVEIE KLYDKPITEV RKIVEGLGTN
     HTIAVTMKKT ELIFLLVKIL SENNIDVLFT GVLDVLSDGY GFLRTASNSY LSGGNDVYVS
     PSQIRLFNLR TGDILYGQIR SPRDGERFFA MVKIKSINDQ DPTFAQNRIP FDNLTPLYPN
     VKLNLEYENC NISTRLINLF SPIGKGQRAL IVSPPKAGKT TLLQKIANAI TTNYSDVILM
     ILLIDERPEE VTDMIRSVKG EVIASNFDEQ ASRHVQVAEM VIEKAKRLVE NKKDVVILLD
     SITRLARAYN QTMPTSGKIL SGGVDSNALH KPKRFFGSAR NIEEGGSLTI IATALVDTGS
     KMDEVIFEEF KSTGNMELIL DRSLADRRLF PAINIKKSGT RKEELLLSEE ERSKILLIRR
     ILGGVDDYEG VEVLIEKMKK SKNNEIFLKT MSNGN