ID   D9Q9U2_CORP2            Unreviewed;       714 AA.
AC   D9Q9U2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   14-DEC-2022, entry version 63.
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=.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., Turk M.Z.,
RA   Seyffert N., Moraes P.M., Soares S.C., Almeida S.S., Castro T.L.,
RA   Abreu V.A., Trost E., Baumbach J., Tauch A., Schneider M.P., McCulloch J.,
RA   Cerdeira L.T., Ramos R.T., Zerlotini A., Dominitini A., Resende D.M.,
RA   Coser E.M., Oliveira L.M., Pedrosa A.L., Vieira C.U., Guimaraes C.T.,
RA   Bartholomeu D.C., Oliveira D.M., Santos F.R., Rabelo E.M., Lobo F.P.,
RA   Franco G.R., Costa A.F., Castro I.M., Dias S.R., Ferro J.A., Ortega J.M.,
RA   Paiva L.V., Goulart L.R., Almeida J.F., Ferro M.I., Carneiro N.P.,
RA   Falcao P.R., 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 strains.";
RL   PLoS ONE 6:E18551-E18551(2011).
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: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, ECO:0000256|PROSITE-ProRule:PRU01203}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01884}.
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DR   EMBL; CP001829; ADL10318.1; -; Genomic_DNA.
DR   RefSeq; WP_013241693.1; NC_017301.2.
DR   AlphaFoldDB; D9Q9U2; -.
DR   STRING; 1719.CPTC_01383; -.
DR   EnsemblBacteria; ADL10318; ADL10318; CpC231_0837.
DR   GeneID; 69459951; -.
DR   KEGG; cpq:CPC231_04210; -.
DR   PATRIC; fig|681645.3.peg.868; -.
DR   eggNOG; COG1158; Bacteria.
DR   HOGENOM; CLU_016377_3_2_11; -.
DR   OMA; TTDLMGA; -.
DR   Proteomes; UP000000276; 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; IPR011112; Rho_N.
DR   InterPro; IPR036269; Rho_N_sf.
DR   InterPro; IPR011113; Rho_RNA-bd.
DR   InterPro; IPR004665; Term_rho.
DR   PANTHER; PTHR46425; TRANSCRIPTION TERMINATION FACTOR RHO; 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; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF68912; Rho N-terminal domain-like; 1.
DR   TIGRFAMs; TIGR00767; rho; 1.
DR   PROSITE; PS51856; RHO_RNA_BD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01884};
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|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Transcription termination {ECO:0000256|ARBA:ARBA00022472,
KW   ECO:0000256|HAMAP-Rule:MF_01884}.
FT   DOMAIN          324..411
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000259|PROSITE:PS51856"
FT   REGION          47..320
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        118..134
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..166
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        167..181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        184..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..252
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        267..294
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         454..459
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         466..471
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="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
//