ID   PRIA_BUCAP              Reviewed;         720 AA.
AC   Q8KA15;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, 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=BUsg_112;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67681.1; -; Genomic_DNA.
DR   RefSeq; WP_011053647.1; NC_004061.1.
DR   AlphaFoldDB; Q8KA15; -.
DR   SMR; Q8KA15; -.
DR   STRING; 198804.BUsg_112; -.
DR   PRIDE; Q8KA15; -.
DR   EnsemblBacteria; AAM67681; AAM67681; BUsg_112.
DR   KEGG; bas:BUsg_112; -.
DR   eggNOG; COG1198; Bacteria.
DR   HOGENOM; CLU_013353_3_1_6; -.
DR   OMA; CHICNDY; -.
DR   OrthoDB; 1132322at2; -.
DR   Proteomes; UP000000416; 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; -; 1.
DR   HAMAP; MF_00983; PriA; 1.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005259; PriA.
DR   InterPro; IPR041222; PriA_3primeBD.
DR   InterPro; IPR042115; PriA_3primeBD_sf.
DR   Pfam; PF17764; PriA_3primeBD; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00595; priA; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 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..720
FT                   /note="Primosomal protein N'"
FT                   /id="PRO_0000102119"
FT   DOMAIN          200..366
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         425..437
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         452..468
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   MOTIF           309..312
FT                   /note="DEAH box"
FT   BINDING         213..220
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ   SEQUENCE   720 AA;  86672 MW;  BBB318AC6700E4CC CRC64;
     MIIVKVVLPL PIRKYFKYFM PDSMCPIIGG RIVVPFRSKD IVGIVISFCN KKNISNLNLA
     FVKSCIDTES IYSDVVFSIL IWLSRYYYFP IGSIFFSILP KYLKKICLID NKNYKFAILR
     KTKYKDFKTF NLLFFCKKKS FIDKDLEKYT FFDFFLKKNF LQKSCKNYFY HENIPHIYQN
     YLIKKKFFLN KKIIFIINKI LMKNCFTSWL ITKNNFYLKV KFYLGLIKEC LSKNLQILIL
     VPFVKDIYQI LFFLKKYFNV YIDIIHSQLN NEDYLKKWIR TKSGKNSIII GTKNSVFFPF
     LKLGLIIVNQ EHHLNYRNLD QCRYNVRDIA ILRAYKQNIP IILDSDTPSL RTLYNILHKK
     CFYIKFIKNK KTFFLKNNVI DLRKERIKIG LSSTLINEIF NNIQKNYPVL LVLNKFSFVF
     FGLICRRCGK IEKCHICNDY FETKKYDNFL FCRNCLIKIK KPLFCYNCKN FSLIVFDFGI
     KKIKNSFKKI FPNINLFFLL SLKKNKTKKL KIQFFKFPIS NACIIITTEK ISQHYYFPYV
     RFIALTNVDH YFFSFHFCSI EHFLQFYFNL INLTGENKKL LKIFIQTSYP NNKFLLNLCS
     SDYFLFCRKI LSLRKKYFLP PWNFQVIFYS SSKFFEKSFI FLECIQIILK KQSKRDNVSL
     WFVGPHPVFS LKDRKKCFYQ LLIHSPSRTY LKKILKESIN IVQCFSISQN VQWFLDIDIY