ID   PRIS_HYPBU              Reviewed;         380 AA.
AC   A2BN97;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=DNA primase small subunit PriS {ECO:0000255|HAMAP-Rule:MF_00700};
DE            EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00700};
GN   Name=priS {ECO:0000255|HAMAP-Rule:MF_00700}; Synonyms=priA;
GN   OrderedLocusNames=Hbut_1644;
OS   Hyperthermus butylicus (strain DSM 5456 / JCM 9403 / PLM1-5).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Hyperthermus.
OX   NCBI_TaxID=415426;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5456 / JCM 9403 / PLM1-5;
RX   PubMed=17350933; DOI=10.1155/2007/745987;
RA   Bruegger K., Chen L., Stark M., Zibat A., Redder P., Ruepp A., Awayez M.,
RA   She Q., Garrett R.A., Klenk H.-P.;
RT   "The genome of Hyperthermus butylicus: a sulfur-reducing, peptide
RT   fermenting, neutrophilic Crenarchaeote growing up to 108 degrees C.";
RL   Archaea 2:127-135(2007).
CC   -!- FUNCTION: Catalytic subunit of DNA primase, an RNA polymerase that
CC       catalyzes the synthesis of short RNA molecules used as primers for DNA
CC       polymerase during DNA replication. The small subunit contains the
CC       primase catalytic core and has DNA synthesis activity on its own.
CC       Binding to the large subunit stabilizes and modulates the activity,
CC       increasing the rate of DNA synthesis while decreasing the length of the
CC       DNA fragments, and conferring RNA synthesis capability. The DNA
CC       polymerase activity may enable DNA primase to also catalyze primer
CC       extension after primer synthesis. May also play a role in DNA repair.
CC       {ECO:0000255|HAMAP-Rule:MF_00700}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00700};
CC   -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit
CC       (PriL). {ECO:0000255|HAMAP-Rule:MF_00700}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit
CC       family. {ECO:0000255|HAMAP-Rule:MF_00700}.
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DR   EMBL; CP000493; ABM81458.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2BN97; -.
DR   SMR; A2BN97; -.
DR   STRING; 415426.Hbut_1644; -.
DR   PRIDE; A2BN97; -.
DR   EnsemblBacteria; ABM81458; ABM81458; Hbut_1644.
DR   KEGG; hbu:Hbut_1644; -.
DR   eggNOG; arCOG04110; Archaea.
DR   HOGENOM; CLU_056123_1_0_2; -.
DR   OMA; GYHVHVR; -.
DR   Proteomes; UP000002593; Chromosome.
DR   GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR   GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR   GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd04860; AE_Prim_S; 1.
DR   HAMAP; MF_00700; DNA_primase_sml_arc; 1.
DR   InterPro; IPR002755; DNA_primase_S.
DR   InterPro; IPR014052; DNA_primase_ssu_euk/arc.
DR   InterPro; IPR023639; DNA_primase_ssu_PriS.
DR   PANTHER; PTHR10536; PTHR10536; 2.
DR   Pfam; PF01896; DNA_primase_S; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-directed RNA polymerase; Magnesium; Manganese;
KW   Metal-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..380
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_1000045499"
FT   ACT_SITE        101
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        103
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   380 AA;  42814 MW;  A2AB84180562E27B CRC64;
     MPRSQDPVMR TRRFLEHLTR KYYERARVKL PGDFSLREFA LQTWTGKSYL RHLSFASTEA
     VHRLLVEKAP RHFYYSSARY DQPGADDMDA KGWRSADLTF DIDADHLPEC SGSIVEVDGG
     IEGKTSFIEE ALCMRAAALR AQILYDILVY ELGFDKSRIA IEFSGHRGFH VTVYLDDFDD
     YAKAGSDVRR EIVNYVKALG LRADVLEPWT MLQVRRGKPI PIPPNVQLAG ARGRVARIIR
     RLALRDGAID IVKAVEGPST TYSEELREYE DKARQLIGVE IDEQVSVDVK RLIRVPYSIN
     GKTGLLVKPV TVDELDEFVV DETLSPFARE PPVRIRVVTS LPSSVTILGN RLKLREGDSP
     RLPAPVAVYL MAKGVAVLAQ