ID   D9Q9U2_CORP2            Unreviewed;       714 AA.
AC   D9Q9U2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   16-OCT-2019, entry version 50.
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; Corynebacteriales; Corynebacteriaceae;
OC   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   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-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   STRING; 1719.CPTC_01383; -.
DR   EnsemblBacteria; ADL10318; ADL10318; CpC231_0837.
DR   KEGG; cpq:CpC231_0837; -.
DR   PATRIC; fig|681645.3.peg.868; -.
DR   HOGENOM; HOG000076952; -.
DR   KO; K03628; -.
DR   OMA; DNYAFIR; -.
DR   Proteomes; UP000000276; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008186; F:RNA-dependent ATPase activity; IEA:InterPro.
DR   GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-UniRule.
DR   CDD; cd01128; rho_factor; 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; 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; 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   DOMAIN       11     53       Rho_N. {ECO:0000259|SMART:SM00959}.
FT   DOMAIN      455    640       AAA. {ECO:0000259|SMART:SM00382}.
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   REGION       47    320       Disordered. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS     89    117       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    118    134       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    135    166       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    167    181       Polar. {ECO:0000256|SAM:MobiDB-lite}.
FT   COMPBIAS    184    202       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    211    252       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    267    294       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
FT   COMPBIAS    305    319       Polyampholyte. {ECO:0000256|SAM:MobiDB-
FT                                lite}.
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
//