ID   PRIA_RHORU              Reviewed;         811 AA.
AC   P05445;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 97.
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};
OS   Rhodospirillum rubrum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Rhodospirillum.
OX   NCBI_TaxID=1085;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2861810; DOI=10.1042/bj2280391;
RA   Falk G., Hampe A., Walker J.E.;
RT   "Nucleotide sequence of the Rhodospirillum rubrum atp operon.";
RL   Biochem. J. 228:391-407(1985).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA26336.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X02499; CAA26334.1; -; Genomic_DNA.
DR   EMBL; X02499; CAA26336.1; ALT_INIT; Genomic_DNA.
DR   PIR; S08579; S08579.
DR   RefSeq; WP_011388977.1; NZ_CP077803.1.
DR   AlphaFoldDB; P05445; -.
DR   SMR; P05445; -.
DR   PRIDE; P05445; -.
DR   OMA; RCHYCGY; -.
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; 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..811
FT                   /note="Primosomal protein N'"
FT                   /id="PRO_0000102130"
FT   DOMAIN          240..406
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   DOMAIN          490..709
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         520..532
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         547..563
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   REGION          130..161
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          431..482
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           349..352
FT                   /note="DEAH box"
FT   COMPBIAS        462..476
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         253..260
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ   SEQUENCE   811 AA;  85575 MW;  D993121582274341 CRC64;
     MAGLPALPPG SRELFPEDAH AEPVVAVLLP LPLAGAYDYK VPAGMARPAV GTLVRVPLGR
     REEIGVVWGA GAGETPPERL KPLIGFPECP PLPAPLRAFI DWVAAYTVQP PGAVLRMALS
     VPAALEAPPP ALGWRRPSAG QRAAGQRAEG QGPLPGGARL SPGRQRVLAV LDDHPGLPFA
     GADLAREAAV GPAVVAAMAK AGLLEAVTRS NEWSPQAPDA DRPGPLLSAD QQAAADGLRT
     ALDQGFSGLL LEGVTGSGKT EVYFEAIAET LRRGRQALVL LPEIALAAQW PRRFADRFGA
     APVQWHSQMG AAARRRAWRA VALGRAPVVV GARSALFLPY PDLGLIIVDE EHDSAFKQEE
     GVPYNARDMA VVRARLGGFP AVLASATPSL ETIENARQGR YRHLVLPRRH GGAEMPEITL
     LDLRRAPPQK WLPTDFAGPG GSEGLAAPGG ANDEAEEQKA PPPSPTASPS PTASPSPMAR
     PARLGWLSPP LITAVEETLA AGEQVLLFLN RRGYAPLTLC RSCGHRLKCP RCTAWLVEHR
     RDGRLRCHHC GYQQPIPETC PACGVADSLA PCGPGVERLA EEAAHRFPKA RMDVAASDTV
     TGPKEAAALA TRIANHDIDL IIGTQIMAKG HHFPLITLVG VVDGDLGLTG GDLRASERTH
     QLLHQVAGRA GRAERPGRVL IQTVDPGHPV MEALASGDPA LFLEVEAAER QALAMPPFGR
     LVALVISGED SARVQAVAAA LGRAAPMGPG LDVLGPVPAP LAMLRGRHRH RLLLKAARGV
     KVQPVVRHWL SLVSIPPGVK VQVDVDPISF L