PRIA_CHLPN
ID PRIA_CHLPN Reviewed; 749 AA.
AC Q9Z6Y2; Q9JQA8;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 142.
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=CPn_0924, CP_0942, CpB0955;
OS Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=83558;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CWL029;
RX PubMed=10192388; DOI=10.1038/7716;
RA Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL Nat. Genet. 21:385-389(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AR39;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J138;
RX PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT Japan and CWL029 from USA.";
RL Nucleic Acids Res. 28:2311-2314(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW-183;
RA Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT other Chlamydia strains based on whole genome sequence analysis.";
RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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; AE001363; AAD19062.1; -; Genomic_DNA.
DR EMBL; AE002161; AAF38725.1; -; Genomic_DNA.
DR EMBL; BA000008; BAA99132.1; -; Genomic_DNA.
DR EMBL; AE009440; AAP98885.1; -; Genomic_DNA.
DR PIR; B86606; B86606.
DR PIR; C72018; C72018.
DR RefSeq; NP_225119.1; NC_000922.1.
DR RefSeq; WP_010883559.1; NZ_LN847257.1.
DR AlphaFoldDB; Q9Z6Y2; -.
DR SMR; Q9Z6Y2; -.
DR STRING; 115711.CP_0942; -.
DR EnsemblBacteria; AAD19062; AAD19062; CPn_0924.
DR EnsemblBacteria; AAF38725; AAF38725; CP_0942.
DR GeneID; 45050980; -.
DR KEGG; cpa:CP_0942; -.
DR KEGG; cpj:priA; -.
DR KEGG; cpn:CPn_0924; -.
DR KEGG; cpt:CpB0955; -.
DR PATRIC; fig|115713.3.peg.1005; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_0_0; -.
DR OrthoDB; 1132322at2; -.
DR Proteomes; UP000000583; Chromosome.
DR Proteomes; UP000000801; 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; 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..749
FT /note="Primosomal protein N'"
FT /id="PRO_0000102121"
FT DOMAIN 224..391
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT DOMAIN 490..658
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 454..466
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 481..498
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 333..336
FT /note="DEAH box"
FT BINDING 237..244
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ SEQUENCE 749 AA; 83648 MW; 23101B02F3B97B4B CRC64;
MGYIESSTFR LYAEVIVGSN INKVLDYGVP ENLEHITKGT AVTISLRGGK KVGVIYQIKT
TTQCKKILPI LGLSDSEIVL PQDLLDLLFW ISQYYFAPLG KTLKLFLPAI SSNVIQPKQH
YRVVLKQSKA KTKEILAKLE VLHPSQGAVL KILLQHASPP GLSSLMETAK VSQSPIHSLE
KLGILDIVDA AQLELQEDLL TFFPPAPKDL HPEQQSAIDK IFSSLKTSQF HTHLLFGITG
SGKTEIYLRA TSEALKQGKS TILLVPEIAL TVQTVSLFKA RFGKDVGVLH HKLSDSDKSR
TWRQASEGSL RILIGPRSAL FCPMKNLGLI IVDEEHDPAY KQTESPPCYH ARDVAVMRGK
LAHATVVLGS ATPSLESYTN ALSGKYVLSR LSSRAAAAHP AKISLINMNL EREKSKTKIL
FSQPVLKKIA ERLEVGEQVL IFFNRRGYHT NVSCTVCKHT LKCPHCDMVL TFHKYANVLL
CHLCNSSPKD LPQSCPKCLG TMTLQYRGSG TEKIEKILQQ IFPQIRTIRI DSDTTKFKGS
HETLLRQFAT GKADVLIGTQ MIAKGMNFSA VTLAVILNGD SGLYIPDFRA SEQVFQLITQ
VAGRSGRSHL PGEILIQSFL PDHPTIHSAM RQDYSAFYSQ EITGRELCEY PPFIRLIRCI
FMGKCPKQTW EEAHRVHNIL KEQLESTNPL MPVTPCGHFK IKDTFRYQFL IKSAYVIPVN
KKLHHALMLA KLSPKVKFMI DVDPMTTFF
