ID   D9Q9U2_CORP2            Unreviewed;       728 AA.
AC   D9Q9U2;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2023, sequence version 2.
DT   02-OCT-2024, entry version 73.
DE   RecName: Full=Transcription termination factor Rho {ECO:0000256|HAMAP-Rule:MF_01884, ECO:0000256|NCBIfam:TIGR00767};
DE            EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01884, ECO:0000256|NCBIfam:TIGR00767};
DE   AltName: Full=ATP-dependent helicase Rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   Name=rho {ECO:0000256|HAMAP-Rule:MF_01884};
GN   ORFNames=CPC231_04210 {ECO:0000313|EMBL:ADL10318.2};
OS   Corynebacterium pseudotuberculosis (strain C231).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=681645 {ECO:0000313|EMBL:ADL10318.2, ECO:0000313|Proteomes:UP000000276};
RN   [1] {ECO:0000313|EMBL:ADL10318.2, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL10318.2,
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:ADL10318.2, ECO:0000313|Proteomes:UP000000276}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C231 {ECO:0000313|EMBL:ADL10318.2,
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; ADL10318.2; -; Genomic_DNA.
DR   AlphaFoldDB; D9Q9U2; -.
DR   STRING; 681645.CpC231_0837; -.
DR   KEGG; cpq:CPC231_04210; -.
DR   PATRIC; fig|681645.3.peg.868; -.
DR   eggNOG; COG1158; Bacteria.
DR   HOGENOM; CLU_016377_3_2_11; -.
DR   Proteomes; UP000000276; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008186; F:ATP-dependent activity, acting on RNA; 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:0006353; P:DNA-templated transcription termination; IEA:UniProtKB-UniRule.
DR   CDD; cd01128; rho_factor_C; 1.
DR   Gene3D; 1.10.720.10; -; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR00767; rho; 1.
DR   PANTHER; PTHR46425; TRANSCRIPTION TERMINATION FACTOR RHO; 1.
DR   PANTHER; PTHR46425:SF1; 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   PROSITE; PS51856; RHO_RNA_BD; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01884};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01884};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01884};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01884}; 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          338..425
FT                   /note="Rho RNA-BD"
FT                   /evidence="ECO:0000259|PROSITE:PS51856"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          61..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..131
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        149..180
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        181..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        198..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        225..266
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        281..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..333
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         468..473
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         480..485
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT   BINDING         511
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ   SEQUENCE   728 AA;  80479 MW;  14C18C110D291653 CRC64;
     MTSFTSGKGD ERTSVTTTDN GAQRNLAALR LPELRKIAAE MGLKGTSALR KGDLIAAISG
     AQGGKAAQSG HSAAPAAKRN ARAQAAPKAE KDSAPVENSV PEVSKEQQEK ADQVPAKESK
     SRRRRVLKTT GTMDSTHETA SSEPISQESS PAEEEKPRRR RVTRRVEVSS EKRDPAENSP
     QDKTDTPSES NDGVARVSEN GDAEDENRYE SRSAARRARR NRARREHRED RQTSQREDNH
     AEGDRSSNDE EQRKEASVDN VKATGRREAS EQQAADQPQT RETREGSENE HPRQRNGRHH
     ERGERGDRNR RNRRNRRGRD RDDHRDNSNI EPREDEVLQN IAGILDIVDS NVAFVRTSGY
     HAGSADVYVN NQMIRRLGLR AGDAITGQVR MNGDNNHGGH HGHNRGRNRQ KYNPLVRVES
     VNGMSVEEAK ARPDFSKLTP LYPNQRLRLE TEPKILTTRV IDLIMPIGKG QRALIVSPPK
     AGKTTILQNI ANAIATNNPE CYLMVVLVDE RPEEVTDMQR SVKGEVIAST FDRPPSEHTA
     VAELAIERAK RLVEQGQDVV VLLDSITRLG RAYNNSSPAS GRILSGGVDS NALYPPKRFL
     GAARNIENGG SLTIIATAMV ETGSAGDTVI FEEFKGTGNA ELKLDRKISE RRVFPAVDVN
     PSGTRKDELL LVPEEARIMH KLRRILAALD NQQAIDLLIK QLKKTKSNGE FLMQIASSAP
     MAADAEEE
//