PRIA_HAEIN
ID PRIA_HAEIN Reviewed; 730 AA.
AC P44647;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 133.
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=HI_0339;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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; L42023; AAC22001.1; -; Genomic_DNA.
DR PIR; G64062; G64062.
DR RefSeq; NP_438503.1; NC_000907.1.
DR RefSeq; WP_005694336.1; NC_000907.1.
DR AlphaFoldDB; P44647; -.
DR SMR; P44647; -.
DR STRING; 71421.HI_0339; -.
DR EnsemblBacteria; AAC22001; AAC22001; HI_0339.
DR KEGG; hin:HI_0339; -.
DR PATRIC; fig|71421.8.peg.356; -.
DR eggNOG; COG1198; Bacteria.
DR HOGENOM; CLU_013353_3_1_6; -.
DR OMA; RCHYCGY; -.
DR PhylomeDB; P44647; -.
DR BioCyc; HINF71421:G1GJ1-355-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0043138; F:3'-5' DNA helicase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; 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:0006310; P:DNA recombination; IBA:GO_Central.
DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
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..730
FT /note="Primosomal protein N'"
FT /id="PRO_0000102124"
FT DOMAIN 212..378
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT DOMAIN 472..640
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 437..449
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 464..480
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 321..324
FT /note="DEAH box"
FT BINDING 225..232
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ SEQUENCE 730 AA; 82336 MW; 5DB1D638426C4714 CRC64;
MKIVRVALAV PLPRLFDYFV PDDVSLQIGM RVLVPFGTQK RVAIVADFPT KSDVPEDKLK
AILQPLDLAP LFTPIYWDWL HWAANYYQAG LGDVLFQALP VKLRNGESAV KNDRTFWRIT
DAGKNALKQG ELKRSKKQAE ALQYLSETDL EKGNNDFSSA IWSALKAKGF IEEITIQTNP
LSWQQRLGNN PIVNAENRLT LNKQQALAFS QLLFHSGFNV WLLDGVTGSG KTEIYLQYIE
EILKSGKQVL VLVPEIGLTP QTVQRFKVRF NVEIDVLHSN LTDTQRLYVW DRARSGQSAI
VIGTRSALFT QFSNLGAIIL DEEHDSSYKQ QDSWRYHARD LAIVLAQKLN ISVLMGSATP
SLESINNVQN GKYQHLVLSK RAGNSTALRH FVIDLKNQNI QNGLSKPLLE RMKAHLEKGN
QVLLFLNRRG FAPVLLCHEC GWIAQCPHCE KPYTYHQHQN VLRCHHCGAQ KTIPRQCGDC
GSTHLVTTGL GTEQLEETLK TLFPHYSVAR IDRDSTSRKG KLEGYLEDIQ QGKSQILIGT
QMLAKGHHFP NVTLVALVNV DSALFSLDFR AEERLAQLYI QVAGRAGRAD KQGEVVLQTH
YPDHPLLTTL LANGYQAFAK ETLQLRHSMG LPPFTFQALI KAQARHSDLA ENCLSQIADF
FQSKQITGLQ MLGPMPAPFS KKAGQYRWQL LLQHPSRMTL QKALREYQQA ELEKNSQVRL
ILDVDPQDLS
