PRIA_TREPA
ID PRIA_TREPA Reviewed; 657 AA.
AC O83258;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 124.
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=TP_0230;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; AE000520; AAC65217.1; -; Genomic_DNA.
DR PIR; D71351; D71351.
DR RefSeq; WP_010881678.1; NC_021490.2.
DR AlphaFoldDB; O83258; -.
DR SMR; O83258; -.
DR STRING; 243276.TPANIC_0230; -.
DR PRIDE; O83258; -.
DR EnsemblBacteria; AAC65217; AAC65217; TP_0230.
DR KEGG; tpa:TP_0230; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_0_12; -.
DR OMA; RCHYCGY; -.
DR OrthoDB; 1132322at2; -.
DR Proteomes; UP000000811; 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; PF00271; Helicase_C; 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; 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..657
FT /note="Primosomal protein N'"
FT /id="PRO_0000102136"
FT DOMAIN 143..309
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT DOMAIN 390..570
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 366..378
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 393..409
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 252..255
FT /note="DEAH box"
FT BINDING 156..163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ SEQUENCE 657 AA; 72168 MW; 64D8423F390577DD CRC64;
MAPWLELVFD VPLDKSFTYR ACAAHAGEAL VGRRVLAPFG ARTLIGFVIS ESHSSPADCG
GAVGTFKEII RVIDREALFD QTHLACARWM AHFYLCALGQ ALCAVVPSRK RERTLSSFAS
CAGVRRTDTY ALSGEQRKAI DAITASTGAR SFYVHGVTGS GKTEVFLRAA EAVLARGKSV
IYLVPEIALT HQVLQEVYVR FGSQAAVLHS ALSGSQRLGE WRRIQCMRHC VVIGARSAIF
APLKRLGLVI MDEEHDSSYK SAHVPRYHAR QVAMYRCADA NCPFVMGSAT PSVEAWYAML
RGAVRRLPLT ARVAGGAPPR VEVVDVSKEA LLLSTRLVDE IRKTKEAGYQ SMLFLNRRGF
SYSFQCRSCG YTLCCTQCAV PLTWHKRVGA MQCHYCGRQE APPESCPCCH SFDTRYGGVG
TEYIEEAVQA LFPEYRIARV DTDALRSGHV QQTMEQFRAG KIDVLLGTQM IAKGFNFPTL
RLVGIACADT GLHTPDFRAA ERSFALMMQV AGRAGRYVDN GLVIIQTRNP AHPAVVCAQH
GDCESFYAQE LAQREALCFP PFVRLIRFVF RSKTRRKAKD AAYAAHALLT AQMPLGADVL
GPAACVVAQV AGSYRMQILL RAPSFPVVQQ VARSFLDEFR APAGVYVESD VDPVNVL
