ID C6XFY0_LIBAP Unreviewed; 423 AA.
AC C6XFY0;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 88.
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:ACT57283.1};
GN OrderedLocusNames=CLIBASIA_03505 {ECO:0000313|EMBL:ACT57283.1};
OS Liberibacter asiaticus (strain psy62).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=537021 {ECO:0000313|EMBL:ACT57283.1, ECO:0000313|Proteomes:UP000002744};
RN [1] {ECO:0000313|EMBL:ACT57283.1, ECO:0000313|Proteomes:UP000002744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX PubMed=19589076; DOI=10.1094/MPMI-22-8-1011;
RA Duan Y., Zhou L., Hall D.G., Li W., Doddapaneni H., Lin H., Liu L.,
RA Vahling C.M., Gabriel D.W., Williams K.P., Dickerman A., Sun Y.,
RA Gottwald T.;
RT "Complete genome sequence of citrus huanglongbing bacterium, 'Candidatus
RT Liberibacter asiaticus' obtained through metagenomics.";
RL Mol. Plant Microbe Interact. 22:1011-1020(2009).
RN [2] {ECO:0000313|EMBL:ACT57283.1, ECO:0000313|Proteomes:UP000002744}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=psy62 {ECO:0000313|Proteomes:UP000002744};
RX PubMed=21784907; DOI=10.1128/AEM.05111-11;
RA Zhou L., Powell C.A., Hoffman M.T., Li W., Fan G., Liu B., Lin H., Duan Y.;
RT "Diversity and plasticity of the intracellular plant pathogen and insect
RT symbiont, 'Candidatus Liberibacter asiaticus', revealed by hyper variable
RT prophage genes with intragenic tandem repeats.";
RL Appl. Environ. Microbiol. 77:6663-6673(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; CP001677; ACT57283.1; -; Genomic_DNA.
DR RefSeq; WP_012778732.1; NC_012985.3.
DR AlphaFoldDB; C6XFY0; -.
DR STRING; 537021.CLIBASIA_03505; -.
DR GeneID; 66285988; -.
DR KEGG; las:CLIBASIA_03505; -.
DR eggNOG; COG1158; Bacteria.
DR HOGENOM; CLU_016377_4_3_5; -.
DR OrthoDB; 9805197at2; -.
DR Proteomes; UP000002744; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProt.
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; cd04459; Rho_CSD; 1.
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 51..126
FT /note="Rho RNA-BD"
FT /evidence="ECO:0000259|PROSITE:PS51856"
FT BINDING 172..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 184..189
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
FT BINDING 215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01884"
SQ SEQUENCE 423 AA; 47517 MW; A61EF5D21DBEF4A9 CRC64;
MSEMKLQELK NKSPTKLLAF AESLEIENAN VMRKQELMFS ILKVLSGRDV EIIGEGVIEV
LQDGFGFLRS PDANYLAGPD DIYVSPSQIK SFSLKTGDTV EGSIRAPREG ERYFALLKVN
AINFDVPERV RNKIHFDNLT PLYPDKRFNM ELNNPENKDI SSRVIDLIAP IGKGQRSLIV
APPRTGKTIL LQNIAHSIKK NHPECYLIVL LIDERPEEVT DMQRSVQGEV ISSTFDESAA
RHVQVAEMVI AKAKCLVEYG LDVVILLDSI TRLCRAYNVL MPSSGKILTG GVDANALQRP
KRFFGAARNI KEGGSLTIIG TALVDTGSRM DEVIFEEFKG TGNSEIVLER KIADKRIFPA
MDIIKSGTRK EDLLVERQDL QKVFMLRRIV SSMNSSDAIE FLIDKLKQTK DNKDFFYSMN
KQN
//
