HRPA_BORBU
ID HRPA_BORBU Reviewed; 823 AA.
AC O51767;
DT 28-MAR-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=ATP-dependent RNA helicase HrpA {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:24367266};
GN Name=hrpA {ECO:0000303|PubMed:21814569};
GN OrderedLocusNames=BB_0827 {ECO:0000312|EMBL:AAC67162.1};
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [2]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=21814569; DOI=10.1371/journal.pone.0022168;
RA Salman-Dilgimen A., Hardy P.O., Dresser A.R., Chaconas G.;
RT "HrpA, a DEAH-box RNA helicase, is involved in global gene regulation in
RT the Lyme disease spirochete.";
RL PLoS ONE 6:E22168-E22168(2011).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF ASP-126; GLU-127; SER-158;
RP THR-160 AND ILE-285.
RX PubMed=24367266; DOI=10.1371/journal.ppat.1003841;
RA Salman-Dilgimen A., Hardy P.O., Radolf J.D., Caimano M.J., Chaconas G.;
RT "HrpA, an RNA helicase involved in RNA processing, is required for mouse
RT infectivity and tick transmission of the Lyme disease spirochete.";
RL PLoS Pathog. 9:E1003841-E1003841(2013).
CC -!- FUNCTION: Has RNA-stimulated ATPase activity and RNA helicase activity
CC (PubMed:24367266). Involved in global regulation of gene expression
CC (PubMed:21814569). Could be involved in RNA processing and post-
CC transcriptional gene regulation (PubMed:24367266). Essential for both
CC tick transmission and mouse infection (PubMed:24367266).
CC {ECO:0000269|PubMed:21814569, ECO:0000269|PubMed:24367266}.
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 Evidence={ECO:0000269|PubMed:24367266};
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene results in the modulation
CC of the expression of about 180 proteins and in a complete loss in the
CC ability of the spirochetes to infect mice by needle inoculation.
CC {ECO:0000269|PubMed:21814569}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH subfamily.
CC {ECO:0000305}.
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DR EMBL; AE000783; AAC67162.1; -; Genomic_DNA.
DR PIR; B70203; B70203.
DR RefSeq; NP_212961.1; NC_001318.1.
DR RefSeq; WP_002660733.1; NC_001318.1.
DR AlphaFoldDB; O51767; -.
DR SMR; O51767; -.
DR STRING; 224326.BB_0827; -.
DR PRIDE; O51767; -.
DR EnsemblBacteria; AAC67162; AAC67162; BB_0827.
DR KEGG; bbu:BB_0827; -.
DR PATRIC; fig|224326.49.peg.1219; -.
DR HOGENOM; CLU_001832_5_12_12; -.
DR OMA; DHDLKRY; -.
DR Proteomes; UP000001807; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF04408; HA2; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 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.
PE 1: Evidence at protein level;
KW ATP-binding; Helicase; Hydrolase; Nucleotide-binding; Reference proteome;
KW Virulence.
FT CHAIN 1..823
FT /note="ATP-dependent RNA helicase HrpA"
FT /id="PRO_0000443809"
FT DOMAIN 16..179
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 203..374
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT MOTIF 126..129
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MUTAGEN 126
FT /note="D->A: Almost loss of ATPase activity and helicase
FT activity. Loss of infectivity in mice."
FT /evidence="ECO:0000269|PubMed:24367266"
FT MUTAGEN 127
FT /note="E->A: Almost loss of ATPase activity and helicase
FT activity. Loss of infectivity in mice."
FT /evidence="ECO:0000269|PubMed:24367266"
FT MUTAGEN 158
FT /note="S->A: Strong decrease of ATPase activity in the
FT presence of poly(A). Strong decrease of helicase activity.
FT Slight delay in the infection in mice."
FT /evidence="ECO:0000269|PubMed:24367266"
FT MUTAGEN 160
FT /note="T->A: Strong decrease of ATPase activity in the
FT presence of poly(A). Strong decrease of helicase activity."
FT /evidence="ECO:0000269|PubMed:24367266"
FT MUTAGEN 285
FT /note="I->A: 4-fold decrease of ATPase activity in the
FT presence of poly(A). ATPase activity is not affected in the
FT absence of poly(A). Almost loss of helicase activity.
FT Decrease of infectivity in mice."
FT /evidence="ECO:0000269|PubMed:24367266"
SQ SEQUENCE 823 AA; 95088 MW; 542298A4202E9E8A CRC64;
MNDFKLPIYK YKDELIKVLK NHNVLIVESP TGSGKTTQLP RIIYEAGFAK LGKIGVTQPR
RIATVSIAEY IAKHIGVNVG EEVGYKIRFE EITSPKTKIK LMTDGVLLQE LKKDTLLYEY
DVIIIDEAHE RSLNIDFILG LIKDISRKRD DFKIIVSSAT INTKIFSKYF NNAPVVSIET
ITYPVQIIYN PPLLNTSKGM ILKIKEIVLN VIKEKKAGDI LIFLSGEKEI KETIKELQEL
NSKKNLIIFP LYGRMPKEAQ EQIFMTTPKN KRKIIVSTNI AETSITIENI KIVIDSGKVK
TNKFQTKTHT YSLQEVPISK SSATQRAGRA GRLSKGTCYR LYKREDYQLR EDYQKEEIYR
TDLSEVVLRM ADIGIRDFTH FDFISKPSTH SIQTASKILK SLDAINNKNE LTEIGKYMIL
FPLIPAHSRA LVEAMINYPQ AIYQTTIGLS FLSTSGIFLL PQNEEMEARQ AHLKYKNPMG
DLIGFVNIFE DFKKALNKEA FTKENYLDLQ GLEEIANVQM QLENIISKLN IPIIQKGVFD
NEGYLKSIMR GMRDYICFKT SKKKYKTIKA QNVIIHPGSL ISTDSVKYFV AGEIIETTKM
YARSIGVLKK EWIDDIILNE EFKHNDISSK ENQITNTGQT KIINEIKIGK KIFKAEYKNN
IYVIKINLET LKEIIFKNEL NNQNNEDLKK IKIQLMHKNI TVFNNKKFLE TIEIVKNMGK
DWHCIKKYET KNVNIDEPEK MKNLLECTMQ FISFPPKKNA LFLSLETDYS GNFRLKPKQN
FIMAIEESIE SIKSLIENKE YIQKLHFIKK LINKVYKKLN YFF
