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   03-AUG-2022, entry version 48.
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; Proteobacteria; 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}.
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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   Gene3D; 3.40.50.300; -; 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   Pfam; PF00270; DEAD; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 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