ID   RHO2_EHRCR              Reviewed;         422 AA.
AC   P0CH93; Q2GFK2;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-OCT-2010, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Transcription termination factor Rho 2 {ECO:0000255|HAMAP-Rule:MF_01884};
DE            EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01884};
DE   AltName: Full=ATP-dependent helicase Rho 2 {ECO:0000255|HAMAP-Rule:MF_01884};
GN   Name=rho2 {ECO:0000255|HAMAP-Rule:MF_01884}; OrderedLocusNames=ECH_0200;
OS   Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=205920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC CRL-10679 / Arkansas;
RX   PubMed=16482227; DOI=10.1371/journal.pgen.0020021;
RA   Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V.,
RA   Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M.,
RA   Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C.,
RA   Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C.,
RA   Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D.,
RA   Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R.,
RA   Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.;
RT   "Comparative genomics of emerging human ehrlichiosis agents.";
RL   PLoS Genet. 2:208-222(2006).
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; CP000236; ABD44973.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0CH93; -.
DR   SMR; P0CH93; -.
DR   EnsemblBacteria; ABD44973; ABD44973; ECH_0200.
DR   KEGG; ech:ECH_0200; -.
DR   HOGENOM; CLU_016377_4_3_5; -.
DR   Proteomes; UP000008320; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
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   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..422
FT                   /note="Transcription termination factor Rho 2"
FT                   /id="PRO_0000398667"
FT   DOMAIN          49..124
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01203"
FT   BINDING         173..178
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT   BINDING         185..190
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
FT   BINDING         216
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01884"
SQ   SEQUENCE   422 AA;  46864 MW;  26D27C8197AE94E3 CRC64;
     MLDLSELKKK TIEDLLKIAE DLGVVSNGRM LKQEIIFHLM KKVVSDGGAA IGGGVVEILS
     DGFGFLRSPE ANYAASGDDV YISAGQIKKF NLRTGDIVSG EIRAPSEKER YFTLVKAHSI
     NFTDMAKLQR YVHFDDLIPL YPEERILLEC NDPISVSKKD ISMRVIDIVA PLGKGQRALI
     VAPPRAGKTI ILQQIAHSIS VNHPDIELIV LLIGERPEEV TDMCRSVKGE VVSSTFDEPG
     YRHVQLAEIV IEKAKRMVEH KKNVVILLDS ITRLARAYNS VIPSSGKVLT GGVDSNALQR
     PKRFFGAARN IENGGSLTII ATALIETGSK MDEVIFEEFK GTGNCEIILD RKISDKRVYP
     AIDISKSGTR KEDMLIDSVC LKKVWLLRRL LSSMGSVEAM EFLRDKLLIT KDNNEFFDMM
     NS