ID PRIA_THEMA Reviewed; 736 AA.
AC Q9WY22;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 27-MAR-2024, entry version 151.
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=TM_0178;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(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}.
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DR EMBL; AE000512; AAD35271.1; -; Genomic_DNA.
DR PIR; H72409; H72409.
DR RefSeq; NP_227993.1; NC_000853.1.
DR RefSeq; WP_004082813.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WY22; -.
DR SMR; Q9WY22; -.
DR STRING; 243274.TM_0178; -.
DR PaxDb; 243274-THEMA_03910; -.
DR EnsemblBacteria; AAD35271; AAD35271; TM_0178.
DR KEGG; tma:TM0178; -.
DR eggNOG; COG1198; Bacteria.
DR InParanoid; Q9WY22; -.
DR OrthoDB; 9759544at2; -.
DR Proteomes; UP000008183; 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 CDD; cd17929; DEXHc_priA; 1.
DR CDD; cd18804; SF2_C_priA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR Gene3D; 3.40.1440.60; PriA, 3(prime) DNA-binding domain; 1.
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 NCBIfam; TIGR00595; priA; 1.
DR PANTHER; PTHR30580; PRIMOSOMAL PROTEIN N; 1.
DR PANTHER; PTHR30580:SF0; PRIMOSOMAL PROTEIN N; 1.
DR Pfam; PF00270; DEAD; 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; P-loop containing nucleoside triphosphate hydrolases; 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..736
FT /note="Primosomal protein N'"
FT /id="PRO_0000102135"
FT DOMAIN 230..396
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT DOMAIN 487..643
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 452..464
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT ZN_FING 479..495
FT /note="C4-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
FT MOTIF 339..342
FT /note="DEAH box"
FT BINDING 243..250
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00983"
SQ SEQUENCE 736 AA; 84557 MW; 138ECBB3260D4C77 CRC64;
MYYKVAVSGS GKVLNVFSSE ELLIGERVWL NWRNGKVKGY VLERSLSHEN EATPSERDGK
SFLSEGHVEI AKWVSERFFS PLGMVFDLFF PQGIDDYKEE VVVSESPFLD FDRMTLRDFL
ENFGEKALKE MVKKGLVRVE KNFYVKEPRP RVKKRLFLKK RISEIIREHL TVKQRMVVEY
LQFNDGVPLE ELLEDLEVSK SVIETLQRKN IVEIVSGDVF PKKRRILRGD FKGNISKENL
FFGPTGSGKT EALFELIDVY SRKGTVLFLV PEVSVLTHTL SRLKGAFPDL KIGIYHSYLS
RARKNLEWYK AASGKIDVLL GTRSAVFVPV KNLSLLIVDE EHDESFYQHT RPSYDAIVVA
RKISEVFDVP IILSSATPDL WTYREAKEGR IRTFNFTRRF GSLSVEVVDM RNEEKIGSFA
KKTLDRIEET LEEGKRVLIY VRRKGFWGRV QCEVCGYVLK CENCDVSLVY HSDTHSLKCH
QCGREYGLVE SCPRCGGRLV GRTAGTERVE RELKRYFPTR RIARVDREVV DNIMELESYI
DKLIRGEIDI LVGTRLITKS LSVPEIGLVC IMDVDSLIFN PDYSSSLRTF QLVVQALGRA
SRGDQGKAII QTYNPEDTII RKALEEDVNG FYAEELERRK ALGYPPYRHL IQVAVKSKNP
EVGKNSLTSL KEFLKGEEVL GPVEHWVFKL RGFYRHHLIV KTEDLERVLP KLEKALRILG
IDAIVRVDPP TLEVSD
//
