位置:首页 > 蛋白库 > PRIA_HELPJ
PRIA_HELPJ
ID   PRIA_HELPJ              Reviewed;         619 AA.
AC   Q9ZKE4;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 131.
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=jhp_0994;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(1999).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE001439; AAD06569.1; -; Genomic_DNA.
DR   PIR; G71861; G71861.
DR   RefSeq; WP_000499292.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZKE4; -.
DR   SMR; Q9ZKE4; -.
DR   STRING; 85963.jhp_0994; -.
DR   TCDB; 3.A.11.3.1; the bacterial competence-related dna transformation transporter (dna-t) family.
DR   EnsemblBacteria; AAD06569; AAD06569; jhp_0994.
DR   KEGG; hpj:jhp_0994; -.
DR   PATRIC; fig|85963.30.peg.1597; -.
DR   eggNOG; COG1198; Bacteria.
DR   OMA; MISKGHD; -.
DR   Proteomes; UP000000804; 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; 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; 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; Zinc; Zinc-finger.
FT   CHAIN           1..619
FT                   /note="Primosomal protein N'"
FT                   /id="PRO_0000102126"
FT   DOMAIN          119..285
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   DOMAIN          371..532
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         336..348
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   ZN_FING         363..379
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT   MOTIF           228..231
FT                   /note="DEAH box"
FT   BINDING         132..139
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ   SEQUENCE   619 AA;  70308 MW;  6062DBF370556CDC CRC64;
     MFYHLIAPLK NKTPPLTYFS KERHLKGALV NIPLRNKTLL GVVLEEVSKP SFECLELEKT
     PYFLLPFQIE LAIFIAQYYS ANLSSVLSLF APFKECDLVG LEKIEPTLNA LSQTQTNALK
     ELQKHPASLL FGDTGSGKTE IYMHAIAQTL EQKKSALLLV PEIALTPQMQ QRLKKVFKEN
     LGLWHSKLSQ NQKKQFLEKL YSQEIKLVVG TRSALFLPLK ELGLIIVDEE HDFSYKSQQS
     PMYNARDLCL YLSHKFPIQV ILGSATPSLS SYQRFKDKAL VRLKGRYTPT QKNIIFEKTE
     RFITPKLLEA LKQVIDKNEQ AIIFVPTRAN FKTLLCPNCY KSVQCPFCSV NMSLHLKTNK
     LMCHYCHFSS PIPKICNACQ SEVLVGKRIG TMQVLKELES LLEGAKIAIL DKDHTSTPKK
     LHNILNDFNA QKTNILIGTQ MISKGHDYAK VSLAVVLGID NIIKSNSYRA LEEGVSLLYQ
     IAGRSARQIS GQVFIQSTET DLLENFLEDY EDFLQYELQE RCELYPPFSR LCLLEFKHKN
     EEKAQQLSLE ASQTLSLCLE KGVTLSNFKA PIEKIASSYR YLILLRSKNP LSLIKSVHAF
     LKTAPNIPCS VNMDPVDIF
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2025