ID J9S609_9ACTN Unreviewed; 701 AA.
AC J9S609;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 ORFNames=KTR9_1851 {ECO:0000313|EMBL:AFR48490.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR48490.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR48490.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR48490.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
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; CP002907; AFR48490.1; -; Genomic_DNA.
DR RefSeq; WP_014926339.1; NC_018581.1.
DR AlphaFoldDB; J9S609; -.
DR STRING; 337191.KTR9_1851; -.
DR KEGG; gor:KTR9_1851; -.
DR PATRIC; fig|337191.3.peg.2128; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_3_0_11; -.
DR Proteomes; UP000003281; 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:InterPro.
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; 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 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; SM00357; CSP; 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};
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 323..401
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 52..322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 153..170
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 444..449
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 456..461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 701 AA; 74763 MW; 4ADCBD06E26858D9 CRC64;
MTDTDLITAP AEQESAGSAG PDSGRPATKT RARTGLSGMV LSELRTVAGE LGIKGTSGMR
KGDLIAAIKE RQAGGDAPAA KSGPTRSKAG SSKPAAADEQ LTIGGDSPAP AGGETAEKAD
APRGTRTQRG AGRKAADADA PISAEAPAGD STPADNKTDS PSTDGVAKNA TTSDAPAADA
AKGGSAPEAD STEAGAGRDR RRGRDGAGDA AADSDGGEQR TRRNRNQNRD NQNRDGGQNR
DNQNRDGGGQ NRDKQNRDGG QNRDNQNRDN QNRDGGQNRD GGQDRDDDGE GGGRRRGRRF
RERRRGQNRD TPNEPQVSDD DVLQPVAGIL DVLDNYAFVR TSGYLAGPND VYVSMNLVRK
NGLRRGDAIT GAVKVPREGD QQNQRQKFNP LVRLDTINGG DVETAKRRPE FNKLTPLYPN
QRLRLETTPE RLDTRVIDLI MPIGKGQRAL IVSPPKAGKT TILQDIANAI ATNNPECHLM
VVLVDERPEE VTDMQRSVKG EVIASTFDRP PSDHTSVSEL AIERAKRLVE SGKDVVVLLD
SITRLGRAYN NASPASGRIL SGGVDSTALY PPKRFLGAAR NIENGGSLTI IASALVETGS
TGDTVIFEEF KGTGNAELKL DRKISERRVF PAVDVNLSST RKDELLLSPE EFSIVHKLRR
VLSGLDSQQA IDLLLSQLKK TKTNMEFLMS VQKTAPGAGN D
//
