ID A0A2H9SJE7_9BACT Unreviewed; 458 AA. AC A0A2H9SJE7; DT 28-FEB-2018, integrated into UniProtKB/TrEMBL. DT 28-FEB-2018, sequence version 1. DT 31-JUL-2019, entry version 11. 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:PJD93847.1}; GN ORFNames=CK425_12275 {ECO:0000313|EMBL:PJD93847.1}; OS Parachlamydia sp. OC Bacteria; Chlamydiae; Parachlamydiales; Parachlamydiaceae; OC Parachlamydia. OX NCBI_TaxID=2052048 {ECO:0000313|EMBL:PJD93847.1, ECO:0000313|Proteomes:UP000237012}; RN [1] {ECO:0000313|EMBL:PJD93847.1, ECO:0000313|Proteomes:UP000237012} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BC.030 {ECO:0000313|EMBL:PJD93847.1}; RX PubMed=29097994; DOI=10.3389/fmicb.2017.02036; RA Zhang Y., Kitajima M., Whittle A.J., Liu W.T.; RT "Benefits of Genomic Insights and CRISPR-Cas Signatures to Monitor RT Potential Pathogens across Drinking Water Production and Distribution RT Systems."; RL Front. Microbiol. 8:2036-2036(2017). 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PJD93847.1}. 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; PEQL01000028; PJD93847.1; -; Genomic_DNA. DR Proteomes; UP000237012; Unassembled WGS sequence. 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; cd04459; Rho_CSD; 1. 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; 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 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; SM00357; CSP; 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:UP000237012}; KW Helicase {ECO:0000256|HAMAP-Rule:MF_01884}; KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01884, KW ECO:0000256|SAAS:SAAS00446781}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01884}; 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 47 89 Rho_N. {ECO:0000259|SMART:SM00959}. FT DOMAIN 95 161 CSP. {ECO:0000259|SMART:SM00357}. FT DOMAIN 210 399 AAA. {ECO:0000259|SMART:SM00382}. FT NP_BIND 209 214 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. FT NP_BIND 221 226 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. FT REGION 1 36 Disordered. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 1 15 Polyampholyte. {ECO:0000256|SAM:MobiDB- FT lite}. FT COMPBIAS 16 36 Polar. {ECO:0000256|SAM:MobiDB-lite}. FT BINDING 252 252 ATP. {ECO:0000256|HAMAP-Rule:MF_01884}. SQ SEQUENCE 458 AA; 51304 MW; 4CDD4F96C3BA08B3 CRC64; MNLENTHEES SSNEETTTSE KMLESQSPGD SSKEQEQIVG EITRIADIQR MNIDQLNQYG KKIGLKHLGS LTKSQMVFEI VKAISENPNE ILYGEGVLEV LPDGFGFLRS PNYNYLPSAE DIYVSPAQIR RFDLKKGDTV CGTIRPPKDK EKYFALLKVD KINGKSPEKA KERILFENLT PLYPNERIVM ETTRDKLSTR VLDLAAPIGK GQRGLIVAPP RSGKTMILQS IANSIATNNP EIVLIVLLID ERPEEVTDMQ RIVVGEVISS TFDEPPERHV QVAEMAIEKA RRLVEHGRDV VILLDSITRL ARAYNTIQPH SGKILTGGID ANALHKPKRF FGAARNIEQG GSLTIIATAL IDTGSRMDEV IFEEFKGTGN MELVLDRRLA DRRIYPAIDL IKSGTRKEEL LYHPNELEKI YLLRQAVADL ASVDAMNLLL GRLKKTNSNV EFLLSMKD //