PRIA_RICTY
ID PRIA_RICTY Reviewed; 648 AA.
AC Q68WJ4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Primosomal protein N' {ECO:0000255|HAMAP-Rule:MF_00983};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_00983};
DE AltName: Full=ATP-dependent helicase PriA {ECO:0000255|HAMAP-Rule:MF_00983};
GN Name=priA {ECO:0000255|HAMAP-Rule:MF_00983}; OrderedLocusNames=RT0529;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
CC -!- FUNCTION: Involved in the restart of stalled replication forks.
CC Recognizes and binds the arrested nascent DNA chain at stalled
CC replication forks. It can open the DNA duplex, via its helicase
CC activity, and promote assembly of the primosome and loading of the
CC major replicative helicase DnaB onto DNA. {ECO:0000255|HAMAP-
CC Rule:MF_00983}.
CC -!- SUBUNIT: Component of the primosome. {ECO:0000255|HAMAP-Rule:MF_00983}.
CC -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00983}.
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DR EMBL; AE017197; AAU03998.1; -; Genomic_DNA.
DR RefSeq; WP_011190979.1; NC_006142.1.
DR AlphaFoldDB; Q68WJ4; -.
DR SMR; Q68WJ4; -.
DR STRING; 257363.RT0529; -.
DR EnsemblBacteria; AAU03998; AAU03998; RT0529.
DR KEGG; rty:RT0529; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_4_1_5; -.
DR OMA; RCHYCGY; -.
DR OrthoDB; 1132322at2; -.
DR Proteomes; UP000000604; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.1440.60; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR HAMAP; MF_00983; PriA; 1.
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; IPR005259; PriA.
DR InterPro; IPR041222; PriA_3primeBD.
DR InterPro; IPR042115; PriA_3primeBD_sf.
DR InterPro; IPR041236; PriA_C.
DR InterPro; IPR040498; PriA_CRR.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; PriA_CRR; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00595; priA; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Metal-binding; Nucleotide-binding; Primosome; Zinc; Zinc-finger.
FT CHAIN 1..648
FT /note="Primosomal protein N'"
FT /id="PRO_0000102133"
FT DOMAIN 131..297
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT DOMAIN 393..548
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 358..370
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 385..401
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 240..243
FT /note="DEAH box"
FT BINDING 144..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ SEQUENCE 648 AA; 73424 MW; FBBE56456EF8B337 CRC64;
MRIAKILLPV SKLFPLDYLI TEDLELNIGD LVVVHFRNQE LTGIVWELAT NSEAKKIKTI
KAKVPLNLNI SLEVLALIKW MSSYYMSELG SIAKLVLPIN IAEKPIKIKE QQVKNYFVLP
QLSEEQKQAV TIFNESNKPT LIKGVTGSGK TEIYFHIIAD HLMKGQQVLI MLPEIALSRQ
IINRFIDRFG FEPIIWNSSV TKAQKKMILR GILSDKVKVV IGARSSLFLP FHNLGLIVID
EEHDDSYKQD DNILYNARDT AIVRGVFDKA KIVLCSATPS LETIYNIKTH KYQLVTLVNR
YKNIDLPNIE IIDMTKEKLP KNSYLSKILI DAIKGNLENK KQVLLFLNRR GYAPLMLCKA
CGHRFTCRFC SAWMVLHKAT KTLECHHCGY QSKIFSSCPE CLEDETLTIC GPGIERIEEE
AMLLFPKSKI AVISKDHAKT PAKIAQLLHQ MENLEIDILI GTQIITKGYH FPNLTLVGVI
DADLGSNNAE LRASERTFQL LHQVGGRAGR GDSKGVVYLQ SYYPDNIIFS YVKVGDEDSF
FTNELEIRKA ANMPPFSKTA SLILSGFSES KILDIAKNIV QIAPKANVKI LGPARALMSK
LAGKYRYRIL IIADKKFNLQ QYLKFWLSLI KIPSYCQIKI DIDPKTFY
