PRIA_RICBR
ID PRIA_RICBR Reviewed; 648 AA.
AC Q1RI08;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=RBE_0925;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE05006.1; -; Genomic_DNA.
DR RefSeq; WP_011477587.1; NC_007940.1.
DR AlphaFoldDB; Q1RI08; -.
DR SMR; Q1RI08; -.
DR STRING; 336407.RBE_0925; -.
DR EnsemblBacteria; ABE05006; ABE05006; RBE_0925.
DR KEGG; rbe:RBE_0925; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_4_0_5; -.
DR OMA; RCHYCGY; -.
DR OrthoDB; 1132322at2; -.
DR Proteomes; UP000001951; 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; 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_0000281069"
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; 73480 MW; 938DCF7E8739303A CRC64;
MQIAKILLSA VKLFPLDYLI PEDLSLNIGD LVVVPFRNKE LTGIVWEFSN VPEVKKLKTI
KEKVPLNLTI TSEVLDLIKW MSNYYMAELG SIAKLVLPVD IAEKPIKVKE QKINNNFTLP
DLSEEQKQAL QMLNDSNKPI LIKGVTGSGK TEVYFYLIAE YLAKGKQALV MLPEIALSTQ
IINRFKERFG FDPIIWNSSV TKAQKKMILR GILEDKVKIV IGARSSLFLP FKNLGLIVID
EEHDDSYKQD DGVLYNARDT AIVRSTFDKA QIVLCSATPS IETMYNANIG KYSVINLSSR
YKNAVLPNIE MIDMTKEELP KNCYLSNILI KAIKNNLENK EQTLLFLNRR GYAPLMLCKS
CGHKFTCKYC SSWMVVHKSS KKLECHHCGY QSKIFNSCPE CLEDESLAIC GPGIERIEEE
AKTLFPNSKI AVISKDHVKN PEKIAQLLHQ MENLEIDILI GTQMITKGYH FPNLTLVGVV
DADLGSNHAD LRSSERAFQL LHQVGGRAGR GNSKGMVYLQ SYYPDNIIFS YIKDEREDNF
FVNELEVRKA ADMPPFSKMA SVILSGTNEH KILEVAKNMV RIAPEAQVKI LGPASSLMSK
LAGKYRFRIL IIADKKFNLQ KYLKFWLELI KIPSFCHIKI DIDPKSFY