RHPA_HELPY
ID RHPA_HELPY Reviewed; 492 AA.
AC O25029;
DT 03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=DEAD-box ATP-dependent RNA helicase RhpA;
DE EC=3.6.4.13;
GN Name=rhpA; OrderedLocusNames=HP_0247, C694_01250;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RA Manolov A., Prihodko E., Larin A., Karpova I., Semashko T., Alexeev D.,
RA Kostrjukova E., Govorun V.;
RT "Draft genome of Helicobacter pylori.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP INTERACTION WITH RNJ, AND SUBUNIT.
RC STRAIN=ATCC 700392 / 26695;
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).
CC {ECO:0000250}.
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. Note=The RNaseJ-RhpA complex co-
CC localizes with 70S ribosomes and polysomes; remains associated with
CC ribosomes in the absence of RNase J. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. {ECO:0000305}.
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DR EMBL; AE000511; AAD07315.1; -; Genomic_DNA.
DR EMBL; CP003904; AFV41471.1; -; Genomic_DNA.
DR PIR; G64550; G64550.
DR RefSeq; NP_207045.1; NC_000915.1.
DR RefSeq; WP_000422563.1; NC_018939.1.
DR AlphaFoldDB; O25029; -.
DR SMR; O25029; -.
DR DIP; DIP-3203N; -.
DR IntAct; O25029; 7.
DR MINT; O25029; -.
DR STRING; 85962.C694_01250; -.
DR PaxDb; O25029; -.
DR PRIDE; O25029; -.
DR EnsemblBacteria; AAD07315; AAD07315; HP_0247.
DR KEGG; heo:C694_01250; -.
DR KEGG; hpy:HP_0247; -.
DR PATRIC; fig|85962.47.peg.267; -.
DR eggNOG; COG0513; Bacteria.
DR HOGENOM; CLU_003041_21_1_7; -.
DR OMA; YDIELYQ; -.
DR PhylomeDB; O25029; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0033592; F:RNA strand annealing activity; IBA:GO_Central.
DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central.
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 Reference proteome; RNA-binding.
FT CHAIN 1..492
FT /note="DEAD-box ATP-dependent RNA helicase RhpA"
FT /id="PRO_0000430105"
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 453..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..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; 55806 MW; C5E35D6C73BB21ED CRC64;
MELNQPPLPT EIDGDAYHKP 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 MDQRDRRSSI
MAFKKNDADV LVATDVASRG LDISGVSHVF NYHLPLNTES YIHRIGRTGR AGKKGMAITL
VTPLEYKELL RMQKEIDSEI ELFEIPTINE NQIIKTLHDA KVSEGIISLY EQLTEIFEPS
QLVLKLLSLQ FETSKIGLNQ QEIDAIQNPK EKTPKPSNKK TPQHERARSF KKGQHRDRHP
KTNHYSKKPK RR