ID   PRIA_RICCN              Reviewed;         648 AA.
AC   Q92HH1;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=RC0800;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03338.1; -; Genomic_DNA.
DR   PIR; H97799; H97799.
DR   RefSeq; WP_010977412.1; NC_003103.1.
DR   AlphaFoldDB; Q92HH1; -.
DR   SMR; Q92HH1; -.
DR   PRIDE; Q92HH1; -.
DR   EnsemblBacteria; AAL03338; AAL03338; RC0800.
DR   KEGG; rco:RC0800; -.
DR   PATRIC; fig|272944.4.peg.909; -.
DR   HOGENOM; CLU_013353_4_0_5; -.
DR   OMA; RCHYCGY; -.
DR   Proteomes; UP000000816; 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_0000102131"
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;  72949 MW;  397ABB89DE8DB6DF CRC64;
     MRIAKILLPV AKLFPLDYLI PEDLELNIGD LVVVPFRNKE LTGIVWELVS NSEAKKIKTI
     RVKVPLNLNI TSEVLELIKW MSSYYMSELG SIAKLVLPMD IAEKPIKVKE QKVNNNFVLP
     DLSEEQKQAV TILNESNKPT LVKGVTGSGK TEIYFHLIAD YLAKGKQVLV MLPEIALSTQ
     IINRFIERFG FEPIIWNSSV TKAHKKMILR GILSDKVKVV IGARSSLFLP FKNLGLIVID
     EEHDDSYKQD DGILYNARDT AIVRGTFDKA QIVLCSATPS IETIHNIEIG KYQLVTLVNR
     YKNVDLPNIE IIDMTKEKLS KNSYLSKLLI EAIKGNLDNK KQVLLFLNRR GYAPLMLCKA
     CGYRLTCKFC SSWMVVHKAT KKLECHHCGY QSKIFSSCPE CLEDETLTIC GPGIERIEEE
     AKALFPESKI AVISKDHAKS PEKIAQLLHQ MENLEIDILI GTQIITKGYH FPNLTLVGVI
     DADLGSNNAD LRASERTFQL LHQVGGRAGR GDSKGVVYLQ SYYPDNTIFS YVKAGDEDSF
     FANELEIRKS ADMPPFSKTA SVILSGSSEA KILEIARDMV RIAPKANVKI LGPASSLMSK
     LAGKYRYRIL IIANKKFNLQ KYLKFWLSLI KIPSFCHLKI DIDPKSFY