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Database: UniProt
Entry: Q45032
LinkDB: Q45032
Original site: Q45032 
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   16-OCT-2019, entry version 127.
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};
GN   OrderedLocusNames=BB_0014;
OS   Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM
OS   4680).
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.,
RA   Saint-Girons I.;
RT   "Borrelia burgdorferi uridine kinase: an enzyme of the pyrimidine
RT   salvage 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 / B31 / CIP 102532 / DSM 4680;
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.,
RA   Gwinn M.L., Dougherty B.A., Tomb J.-F., Fleischmann R.D.,
RA   Richardson D.L., Peterson J.D., Kerlavage A.R., Quackenbush J.,
RA   Salzberg S.L., Hanson M., van Vugt R., Palmer N., Adams M.D.,
RA   Gocayne J.D., Weidman J.F., Utterback T.R., Watthey L., McDonald L.A.,
RA   Artiach P., Bowman C., Garland S.A., Fujii C., Cotton M.D., Horst K.,
RA   Roberts K.M., Hatch B., Smith H.O., Venter J.C.;
RT   "Genomic sequence of a Lyme disease spirochaete, Borrelia
RT   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-
CC       Rule:MF_00983}.
CC   -!- SIMILARITY: Belongs to the helicase family. PriA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00983}.
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   SMR; Q45032; -.
DR   PRIDE; Q45032; -.
DR   EnsemblBacteria; AAC66393; AAC66393; BB_0014.
DR   GeneID; 1194850; -.
DR   KEGG; bbu:BB_0014; -.
DR   PATRIC; fig|224326.49.peg.412; -.
DR   eggNOG; ENOG4105C25; Bacteria.
DR   eggNOG; COG1198; LUCA.
DR   KO; K04066; -.
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: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; 1.10.8.630; -; 1.
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; Complete proteome; DNA replication; DNA-binding;
KW   Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Primosome;
KW   Reference proteome; Zinc; Zinc-finger.
FT   CHAIN         1    660       Primosomal protein N'.
FT                                /FTId=PRO_0000102117.
FT   DOMAIN      145    313       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00983}.
FT   DOMAIN      405    557       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00983}.
FT   NP_BIND     158    165       ATP. {ECO:0000255|HAMAP-Rule:MF_00983}.
FT   ZN_FING     370    382       C4-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00983}.
FT   ZN_FING     397    413       C4-type. {ECO:0000255|HAMAP-
FT                                Rule:MF_00983}.
FT   MOTIF       256    259       DEAH box.
FT   CONFLICT    126    126       P -> L (in Ref. 1; CAA66080).
FT                                {ECO:0000305}.
FT   CONFLICT    555    555       D -> N (in Ref. 1; CAA66080).
FT                                {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
//
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