ID D9Q9U2_CORP2 Unreviewed; 714 AA. AC D9Q9U2; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 27-MAY-2015, entry version 30. 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 ECO:0000313|EMBL:ADL10318.1}; GN OrderedLocusNames=CpC231_0837 {ECO:0000313|EMBL:ADL10318.1}; OS Corynebacterium pseudotuberculosis (strain C231). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Corynebacteriaceae; Corynebacterium. OX NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL10318.1, ECO:0000313|Proteomes:UP000000276}; RN [1] {ECO:0000313|EMBL:ADL10318.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10318.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21037006; DOI=10.1128/JB.01211-10; RG Consortium: Rede Paraense de Genomica e Proteomica (RPGP); RA Silva A., Schneider M.P., Cerdeira L., Barbosa M.S., Ramos R.T., RA Carneiro A.R., Santos R., Lima M., D'Afonseca V., Almeida S.S., RA Santos A.R., Soares S.C., Pinto A.C., Ali A., Dorella F.A., Rocha F., RA de Abreu V.A., Trost E., Tauch A., Shpigel N., Miyoshi A., Azevedo V.; RT "Complete genome sequence of Corynebacterium pseudotuberculosis I19, a RT strain isolated from a cow in Israel with bovine mastitis."; RL J. Bacteriol. 193:323-324(2011). RN [2] {ECO:0000313|EMBL:ADL10318.1, ECO:0000313|Proteomes:UP000000276} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C231 {ECO:0000313|EMBL:ADL10318.1, RC ECO:0000313|Proteomes:UP000000276}; RX PubMed=21533164; DOI=10.1371/journal.pone.0018551; RA Ruiz J.C., D'Afonseca V., Silva A., Ali A., Pinto A.C., Santos A.R., RA Rocha A.A., Lopes D.O., Dorella F.A., Pacheco L.G., Costa M.P., RA Turk M.Z., Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., RA Castro T.L., Abreu V.A., Trost E., Baumbach J., Tauch A., RA Schneider M.P., McCulloch J., Cerdeira L.T., Ramos R.T., Zerlotini A., RA Dominitini A., Resende D.M., Coser E.M., Oliveira L.M., Pedrosa A.L., RA Vieira C.U., Guimaraes C.T., Bartholomeu D.C., Oliveira D.M., RA Santos F.R., Rabelo E.M., Lobo F.P., Franco G.R., Costa A.F., RA Castro I.M., Dias S.R., Ferro J.A., Ortega J.M., Paiva L.V., RA Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P., Falcao P.R., RA Grynberg P., Teixeira S.M., Brommonschenkel S., Oliveira S.C., RA Meyer R., Moore R.J., Miyoshi A., Oliveira G.C., Azevedo V.; RT "Evidence for reductive genome evolution and lateral acquisition of RT virulence functions in two Corynebacterium pseudotuberculosis RT strains."; RL PLoS ONE 6:E18551-E18551(2011). CC -!- FUNCTION: Facilitates transcription termination by a mechanism CC that involves Rho binding to the nascent RNA, activation of Rho's CC RNA-dependent ATPase activity, and release of the mRNA from the CC DNA 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001829; ADL10318.1; -; Genomic_DNA. DR RefSeq; WP_013241693.1; NC_017301.1. DR RefSeq; YP_005683196.1; NC_017301.1. DR EnsemblBacteria; ADL10318; ADL10318; CpC231_0837. DR GeneID; 12299245; -. DR KEGG; cpq:CpC231_0837; -. DR PATRIC; 42899993; VBICorPse140234_0868. DR HOGENOM; HOG000076952; -. DR KO; K03628; -. DR OMA; PLQSIDS; -. DR BioCyc; CPSE681645:GLBW-876-MONOMER; -. DR Proteomes; UP000000276; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 2. 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; IPR011112; Rho_N. DR InterPro; IPR011113; Rho_RNA-bd. DR InterPro; IPR004665; Term_rho. 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; SM00959; Rho_N; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF68912; SSF68912; 1. DR TIGRFAMs; TIGR00767; rho; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01884}; KW Complete proteome {ECO:0000313|Proteomes:UP000000276}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01884}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01884}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01884}; KW Reference proteome {ECO:0000313|Proteomes:UP000000276}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_01884}; KW Transcription {ECO:0000256|HAMAP-Rule:MF_01884}; KW Transcription regulation {ECO:0000256|HAMAP-Rule:MF_01884}; KW Transcription termination {ECO:0000256|HAMAP-Rule:MF_01884}. FT NP_BIND 454 459 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. FT NP_BIND 466 471 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. FT BINDING 497 497 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. SQ SEQUENCE 714 AA; 79026 MW; 4FE1C8AEA6395862 CRC64; MTTTDNGAQR NLAALRLPEL RKIAAEMGLK GTSALRKGDL IAAISGAQGG KAAQSGHSAA PAAKRNARAQ AAPKAEKDSA PVENSVPEVS KEQQEKADQV PAKESKSRRR RVLKTTGTMD STHETASSEP ISQESSPAEE EKPRRRRVTR RVEVSSEKRD PAENSPQDKT DTPSESNDGV ARVSENGDAE DENRYESRSA ARRARRNRAR REHREDRQTS QREDNHAEGD RSSNDEEQRK EASVDNVKAT GRREASEQQA ADQPQTRETR EGSENEHPRQ RNGRHHERGE RGDRNRRNRR NRRGRDRDDH RDNSNIEPRE DEVLQNIAGI LDIVDSNVAF VRTSGYHAGS ADVYVNNQMI RRLGLRAGDA ITGQVRMNGD NNHGGHHGHN RGRNRQKYNP LVRVESVNGM SVEEAKARPD FSKLTPLYPN QRLRLETEPK ILTTRVIDLI MPIGKGQRAL IVSPPKAGKT TILQNIANAI ATNNPECYLM VVLVDERPEE VTDMQRSVKG EVIASTFDRP PSEHTAVAEL AIERAKRLVE QGQDVVVLLD SITRLGRAYN NSSPASGRIL SGGVDSNALY PPKRFLGAAR NIENGGSLTI IATAMVETGS AGDTVIFEEF KGTGNAELKL DRKISERRVF PAVDVNPSGT RKDELLLVPE EARIMHKLRR ILAALDNQQA IDLLIKQLKK TKSNGEFLMQ IASSAPMAAD AEEE //