PRIA_BUCAI
ID PRIA_BUCAI Reviewed; 726 AA.
AC P57220;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=BU120;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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=BAB12838.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000003; BAB12838.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_239952.2; NC_002528.1.
DR RefSeq; WP_010895957.1; NC_002528.1.
DR AlphaFoldDB; P57220; -.
DR SMR; P57220; -.
DR STRING; 107806.10038803; -.
DR EnsemblBacteria; BAB12838; BAB12838; BAB12838.
DR KEGG; buc:BU120; -.
DR PATRIC; fig|107806.10.peg.129; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_6; -.
DR OMA; RCHYCGY; -.
DR Proteomes; UP000001806; 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 InterPro; IPR041236; PriA_C.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 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; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..726
FT /note="Primosomal protein N'"
FT /id="PRO_0000102118"
FT DOMAIN 210..373
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 431..443
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 458..474
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 316..319
FT /note="DEAH box"
SQ SEQUENCE 726 AA; 85642 MW; 06EAB856DC5C1ABE CRC64;
MIIVKVILPI PIRQYFTYLM PDFMCPIIGG RILVPFNSKD VIGIVASFYK KNNVDQANFK
HIKALIDTES LYSNMVLDII SWISNNYHCP AGNLFFSILP KILHSDYIIK NKYICQWSIT
KKGQELNLNY FKRRKKQLYV LLILKKKHIL STELKKYNIS KIILKKLEIQ ELCKVNLNYK
ISFKRKIIRT KKKLFFNKKI SIVLNDVLKK QCFSSWLLTR VNLYLKVKFY LGLIQSVLYK
GVQILILVPY IKNINTIAFF LEKYFNASID VMHSKLTSSK YFSNWVRTKN GENSIVIGTG
KSIFLPFLKL GLIILLEEHN LKYKSINQCR YNIRDLGILR AYKEKIPIIL DSETPSLKTL
NNVLHRKCFY IKLNKYNHVN QINNNIINLK TEKIKFGLSL TLINEIYKNF TGKQVLLIFN
KFVLFFFVLM CQKCNEIFKC TNCDDYFEIN QYRNILFCKF CLIQIKKPIF CYNCGSFSLI
VFKIGAEEIK KEMHSIFPKI PFFFFLNEKN INKNILNTKS FEFAISSPCI IIVTEELVQN
YYFPHVKLIS LICIDNYFLS FNYRAMEYFA QFYINLNQLT RSTKKSCKIF IQTSFPNDIN
LKEICNNGYF SFSKKAMAIR KSFLLPPWSF QTIVYSASTN TKYNIIFLSL MRKILQKKSR
KYNCFLWVLG PNNAFLSINK HKYFHQLLIQ CSSRVALNNV LNESIDVINI FTISKRVKWF
IDIEPN