ID   PRIA_RICPR              Reviewed;         648 AA.
AC   Q9ZD10;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=RP540;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235272; CAA14989.1; -; Genomic_DNA.
DR   PIR; C71658; C71658.
DR   RefSeq; NP_220913.1; NC_000963.1.
DR   RefSeq; WP_004597830.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZD10; -.
DR   SMR; Q9ZD10; -.
DR   STRING; 272947.RP540; -.
DR   EnsemblBacteria; CAA14989; CAA14989; CAA14989.
DR   GeneID; 57569664; -.
DR   KEGG; rpr:RP540; -.
DR   PATRIC; fig|272947.5.peg.551; -.
DR   eggNOG; COG1198; Bacteria.
DR   HOGENOM; CLU_013353_4_1_5; -.
DR   OMA; RCHYCGY; -.
DR   Proteomes; UP000002480; 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; Reference proteome; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..648
FT                   /note="Primosomal protein N'"
FT                   /id="PRO_0000102132"
FT   DOMAIN          131..297
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   DOMAIN          375..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;  73539 MW;  8417C5F831CC86B3 CRC64;
     MRIAKILLPV SKLFPLDYLI TEDLELNIGD LVVVHFRNKE LTGIVWELDT NSEAKKIKTI
     EAKAPLNLSI TLEVLELIKW MSSYYMSELG SIAKLVLPIN ISEKPIKIKE QQVKNHFVLP
     KLSEEQKQAV TILNESNKPT LIKGVTGSGK TEIYFHIIAD YLIKGRQVLI MLPEIALGKQ
     IINRFIDRFG FEPIIWNSSV TKAQKKMILR GILSNKVKVV IGTRSSLFLP FHNLGLIVID
     EEHDDSYKQD DNILYNARDT AIVRGKFDKA KIVLCSATPS LETIYNIKTH KYQLVTLANR
     YKNVDLPNIE IIDMTKEKLP KNSYLSKILI DAIKGNLENK KQALLFLNRR GYAPLMLCKA
     CGHRFTCKFC SAWMVLHKAT KKLECHHCGY QSKIFSSCPE CLEDETLTIC GPGIERIAEE
     AMLLFPKSKI AVISKDHAKT PEKIAQLLHQ MENLEIDILI GTQIITKGYH FPNLTLVGVI
     DADLGSNNAE LRASERTFQL LHQVGGRAGR GDSKGVVYLQ SYYPDNIIFS YVKVGDEDRF
     FTNELEIRKA ANMPPFSKTA SLILSGFSES KILDIARKIV QIAPKANVKI LGPARSLMSK
     LAGKYRYRIL IIADKKFNLQ KYLKFWLGFI KIPSYCQIKI DIDPKTFY