ID RHPA_HELP8 Reviewed; 492 AA. AC B9XXL6; DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 1. DT 28-JUN-2023, entry version 52. DE RecName: Full=DEAD-box ATP-dependent RNA helicase RhpA; DE EC=3.6.4.13; GN Name=rhpA; ORFNames=HPB128_21g22; OS Helicobacter pylori (strain B128). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=544406; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=B128; RX PubMed=19123947; DOI=10.1186/1471-2164-10-3; RA McClain M.S., Shaffer C.L., Israel D.A., Peek R.M. Jr., Cover T.L.; RT "Genome sequence analysis of Helicobacter pylori strains associated with RT gastric ulceration and gastric cancer."; RL BMC Genomics 10:3-3(2009). RN [2] RP FUNCTION AS AN ATPASE, INTERACTION WITH RNJ, SUBUNIT, SUBCELLULAR LOCATION, RP AND DISRUPTION PHENOTYPE. RC STRAIN=B128; RX PubMed=23093592; DOI=10.1093/nar/gks945; RA Redko Y., Aubert S., Stachowicz A., Lenormand P., Namane A., Darfeuille F., RA Thibonnier M., De Reuse H.; RT "A minimal bacterial RNase J-based degradosome is associated with RT translating ribosomes."; RL Nucleic Acids Res. 41:288-301(2013). CC -!- FUNCTION: DEAD-box RNA helicase probably involved in RNA degradation. CC Unwinds dsRNA in both 5'- and 3'-directions (By similarity). Background CC RNA-dependent ATPase activity is stimulated about 5-fold by RNaseJ CC (rnj). Stimulates the dsRNase activity of RNase J. {ECO:0000250, CC ECO:0000269|PubMed:23093592}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; CC -!- SUBUNIT: Homodimer (By similarity). Interacts with RNase J (rnj), might CC be a member of a minimal RNA degradosome complex. {ECO:0000250, CC ECO:0000269|PubMed:23093592}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23093592}. Note=The CC RNaseJ-RhpA complex co-localizes with 70S ribosomes and polysomes; CC remains associated with ribosomes in the absence of RNase J. CC -!- DISRUPTION PHENOTYPE: Not essential, it can be deleted. RNase J remains CC associated with the ribosomes and polysomes. CC {ECO:0000269|PubMed:23093592}. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}. 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; ABSY01000001; EEC25260.1; -; Genomic_DNA. DR RefSeq; WP_000422528.1; NZ_CP024951.1. DR AlphaFoldDB; B9XXL6; -. DR SMR; B9XXL6; -. DR PHI-base; PHI:8011; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC. DR CDD; cd00268; DEADc; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR PANTHER; PTHR47959:SF1; ATP-DEPENDENT RNA HELICASE DBPA; 1. DR PANTHER; PTHR47959; ATP-DEPENDENT RNA HELICASE RHLE-RELATED; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 1: Evidence at protein level; KW ATP-binding; Cytoplasm; Helicase; Hydrolase; Nucleotide-binding; KW RNA-binding. FT CHAIN 1..492 FT /note="DEAD-box ATP-dependent RNA helicase RhpA" FT /id="PRO_0000430106" FT DOMAIN 51..220 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 231..393 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT REGION 445..492 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 20..48 FT /note="Q motif" FT MOTIF 168..171 FT /note="DEAD box" FT COMPBIAS 461..492 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 64..71 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" SQ SEQUENCE 492 AA; 55845 MW; 0EA636F0110D3183 CRC64; MELNQPPLPT EIDDDAYHKP SFNDLGLKES VLKSVYEAGF TSPSPIQEKA IPAVLQGRDV IAQAQTGTGK TAAFALPIIN NLKNNHTIEA LVITPTRELA MQISDEIFKL GKHTRTKTVC VYGGQSVKKQ CEFIKKNPQV MIATPGRLLD HLKNERIHKF VPKVVVLDES DEMLDMGFLD DIEEIFDYLP SEAQILLFSA TMPEPIKRLA DKILENPIKI HIAPSNITNT DITQRFYVIN EHERAEAIMR LLDTQAPKKS IVFTRTKKEA DELHQFLASK NYKSTALHGD MDQRDRRASI MAFKKNDADV LVATDVASRG LDISGVSHVF NYHLPLNTES YIHRIGRTGR AGKKGMAITL VTPLEYKELL RMQKEIDSEI ELFEIPTINE NQIIKTLHDA KVSEGIISLY EQLTEIFEPS QLVLKLLSLQ FETSKIGLNQ QEIDAIQNPK EKTPKPSHKK TPQHERARSF KKGQHRDRHP KTNHHSKKPK RR //