PRIA_BORBU
ID PRIA_BORBU Reviewed; 660 AA.
AC Q45032; O51047;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 138.
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=BB_0014;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=HB19;
RX PubMed=9228761; DOI=10.1111/j.1574-6968.1997.tb12579.x;
RA Boursaux-Eude C., Margarita D., Gilles A.M., Barzu O., Saint-Girons I.;
RT "Borrelia burgdorferi uridine kinase: an enzyme of the pyrimidine salvage
RT pathway for endogenous use of nucleotides.";
RL FEMS Microbiol. Lett. 151:257-261(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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; X97449; CAA66080.1; -; Genomic_DNA.
DR EMBL; AE000783; AAC66393.1; -; Genomic_DNA.
DR PIR; F70101; F70101.
DR RefSeq; NP_212148.1; NC_001318.1.
DR RefSeq; WP_002659035.1; NC_001318.1.
DR AlphaFoldDB; Q45032; -.
DR SMR; Q45032; -.
DR STRING; 224326.BB_0014; -.
DR EnsemblBacteria; AAC66393; AAC66393; BB_0014.
DR KEGG; bbu:BB_0014; -.
DR PATRIC; fig|224326.49.peg.412; -.
DR HOGENOM; CLU_013353_4_1_12; -.
DR OMA; RCHYCGY; -.
DR Proteomes; UP000001807; 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; IPR006935; Helicase/UvrB_N.
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; PF00271; Helicase_C; 1.
DR Pfam; PF17764; PriA_3primeBD; 1.
DR Pfam; PF18074; PriA_C; 1.
DR Pfam; PF18319; PriA_CRR; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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; Reference proteome; Zinc;
KW Zinc-finger.
FT CHAIN 1..660
FT /note="Primosomal protein N'"
FT /id="PRO_0000102117"
FT DOMAIN 145..313
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT DOMAIN 405..557
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 370..382
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 397..413
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 256..259
FT /note="DEAH box"
FT BINDING 158..165
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT CONFLICT 126
FT /note="P -> L (in Ref. 1; CAA66080)"
FT /evidence="ECO:0000305"
FT CONFLICT 555
FT /note="D -> N (in Ref. 1; CAA66080)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 660 AA; 77551 MW; 7F1AB19E04F0EFC3 CRC64;
MVEHYHSTYY YEIAINIPLN KLFFYKFNLN LEIGIRVMVN FNGSNKIGII IKKYFENEFK
EKFEFKIKEI IKIIDTTKII TEHNIDLAHW ISKKTFSGFG ETLFFGLPQN SKAKKNQTLP
SINEHPDHKK CLELNNEQQN IYKEIIGSEK TNVFYLFGIP GSGKTEIFIK LCEYYLALEQ
QVLFLIPEIS LGYQIIKRIK YALNMHHKIY EYNSKVPNSD KNLIWNKVKN GESLVVIGIK
SVLMLPFTKL KLIIMDEEHE TTYKSENIPR FHSRHISFFL QKKFNAKFVM GSATPSLEAY
HAMKNNQIKK IIMQNKFSQS KIEDIKIINM KKEPSTISSE LLYSIQKSLN EKRQSLIFIN
KRGYLKNLEC NECGHIICCP NCSFGLIYHK KENKLLCHYC SYKTKTASHC PQCESKDIKY
KTYGIQLVEK ELKKFLPNAK IARIDSDITK IENIDSINKF ENKEIDILIG TQIIAKGFNF
ENIKTLGIIN ADIGMGLPDF RSGERIFTTL SQIMGRAARF KDDNIIIIQT KNPNYYAIKY
AYKNQYEQFY EEELDIRKKL NYPPFNKIIR IIFRSKNEES AKQKCWEFFE KSKEFLQEEI
EHLGPSEAIM KKISKNYRYN IIYLSKSYSL LEKLVNKTKE KVKMTSTVYI EIDYYPISLI
