ID   PRIS_METTP              Reviewed;         395 AA.
AC   A0B688;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Mthe_0420;
OS   Methanothrix thermoacetophila (strain DSM 6194 / JCM 14653 / NBRC 101360 /
OS   PT) (Methanosaeta thermophila).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanotrichales; Methanotrichaceae; Methanothrix.
OX   NCBI_TaxID=349307;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6194 / JCM 14653 / NBRC 101360 / PT;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P.,
RA   Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Smith K.S., Ingram-Smith C., Richardson P.;
RT   "Complete sequence of Methanosaeta thermophila PT.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000477; ABK14212.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0B688; -.
DR   SMR; A0B688; -.
DR   STRING; 349307.Mthe_0420; -.
DR   EnsemblBacteria; ABK14212; ABK14212; Mthe_0420.
DR   KEGG; mtp:Mthe_0420; -.
DR   HOGENOM; CLU_056123_1_0_2; -.
DR   OMA; GYHVHVR; -.
DR   Proteomes; UP000000674; 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; 1.
DR   Pfam; PF01896; DNA_primase_S; 1.
DR   TIGRFAMs; TIGR00335; primase_sml; 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..395
FT                   /note="DNA primase small subunit PriS"
FT                   /id="PRO_1000045508"
FT   ACT_SITE        95
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        97
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
FT   ACT_SITE        302
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00700"
SQ   SEQUENCE   395 AA;  44848 MW;  CE5B64C0207E9457 CRC64;
     MESKTSTYLR ARFREYYLTA SMDAPPGMEA REWGFIFYDT PGMRRHRSFR SRKELVDYIR
     STVPAHVYHS AAYYLKPDAP TMKEKIWKGA DLIFDLDADH LAEYRGSGIR DFREMLERVK
     GETMKLLEFL LSDFGFDERM ISVAFSGGRG YHIHVRDKSV LKLRSDARRE IVDYLTGRGL
     DPERFIHKIG VDGDAGVERA RSLRGPASDA PGWGGRINKA IESMVMHLRE LDDEEALRLL
     KNVKGIGKQK ARLFLSQIRE ENAIKSIRAG NLDFFKHASG IWNLIIPYIM EETVRALGGE
     TDEPVTADVH RLIRFPESLH GGTGLRVTSL SINSLHAFDP LKDAVVFGDD PVHVEIIRPT
     TLELMGERFD LLEGKTELPE YAAVFLLARG FAEVG