ID RPO12_SACS2 Reviewed; 48 AA. AC Q97ZX7; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 1. DT 08-NOV-2023, entry version 108. DE RecName: Full=DNA-directed RNA polymerase subunit Rpo12 {ECO:0000255|HAMAP-Rule:MF_00615}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00615}; DE AltName: Full=DNA-directed RNA polymerase subunit P {ECO:0000255|HAMAP-Rule:MF_00615}; GN Name=rpo12 {ECO:0000255|HAMAP-Rule:MF_00615}; GN Synonyms=rpoP {ECO:0000255|HAMAP-Rule:MF_00615}; GN OrderedLocusNames=SSO5865; OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) OS (Sulfolobus solfataricus). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Saccharolobus. OX NCBI_TaxID=273057; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2; RX PubMed=11427726; DOI=10.1073/pnas.141222098; RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.; RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2."; RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001). RN [2] {ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ} RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) OF THE RNA POLYMERASE COMPLEX IN RP COMPLEX WITH ZINC, COFACTOR, AND SUBUNIT. RX PubMed=18235446; DOI=10.1038/nature06530; RA Hirata A., Klein B.J., Murakami K.S.; RT "The X-ray crystal structure of RNA polymerase from Archaea."; RL Nature 451:851-854(2008). CC -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the CC transcription of DNA into RNA using the four ribonucleoside CC triphosphates as substrates. {ECO:0000255|HAMAP-Rule:MF_00615}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA- CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_00615}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00615, ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ, CC ECO:0007744|PDB:3HKZ}; CC Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00615, CC ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ, CC ECO:0007744|PDB:3HKZ}; CC -!- SUBUNIT: Part of the 13-subunit RNA polymerase complex. CC {ECO:0000269|PubMed:18235446}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00615}. CC -!- SIMILARITY: Belongs to the archaeal Rpo12/eukaryotic RPC10 RNA CC polymerase subunit family. {ECO:0000255|HAMAP-Rule:MF_00615}. 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; AE006641; AAK40770.1; -; Genomic_DNA. DR PIR; C90189; C90189. DR RefSeq; WP_009988725.1; NC_002754.1. DR PDB; 2PMZ; X-ray; 3.40 A; P/Z=1-48. DR PDB; 3HKZ; X-ray; 3.40 A; P/X=1-48. DR PDBsum; 2PMZ; -. DR PDBsum; 3HKZ; -. DR AlphaFoldDB; Q97ZX7; -. DR SMR; Q97ZX7; -. DR DIP; DIP-60645N; -. DR IntAct; Q97ZX7; 1. DR STRING; 273057.SSO5865; -. DR PaxDb; 273057-SSO5865; -. DR EnsemblBacteria; AAK40770; AAK40770; SSO5865. DR GeneID; 8761752; -. DR KEGG; sso:SSO5865; -. DR PATRIC; fig|273057.12.peg.438; -. DR eggNOG; arCOG04341; Archaea. DR HOGENOM; CLU_179456_2_0_2; -. DR InParanoid; Q97ZX7; -. DR PhylomeDB; Q97ZX7; -. DR BRENDA; 2.7.7.6; 6163. DR EvolutionaryTrace; Q97ZX7; -. DR Proteomes; UP000001974; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IDA:UniProtKB. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR Gene3D; 2.20.28.30; RNA polymerase ii, chain L; 1. DR HAMAP; MF_00615; RNApol_arch_Rpo12; 1. DR InterPro; IPR006591; RNAP_P/RPABC4. DR InterPro; IPR029040; RPABC4/Spt4. DR InterPro; IPR023464; Rpo12. DR SMART; SM00659; RPOLCX; 1. DR SUPFAM; SSF63393; RNA polymerase subunits; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase; Metal-binding; KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase; KW Zinc. FT CHAIN 1..48 FT /note="DNA-directed RNA polymerase subunit Rpo12" FT /id="PRO_0000159767" FT BINDING 9 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615, FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ, FT ECO:0007744|PDB:3HKZ" FT BINDING 12 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:18235446, FT ECO:0007744|PDB:2PMZ, ECO:0007744|PDB:3HKZ" FT BINDING 26 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615, FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ, FT ECO:0007744|PDB:3HKZ" FT BINDING 29 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615, FT ECO:0000269|PubMed:18235446, ECO:0007744|PDB:2PMZ, FT ECO:0007744|PDB:3HKZ" FT STRAND 10..12 FT /evidence="ECO:0007829|PDB:3HKZ" FT STRAND 22..24 FT /evidence="ECO:0007829|PDB:2PMZ" FT STRAND 43..46 FT /evidence="ECO:0007829|PDB:2PMZ" SQ SEQUENCE 48 AA; 5597 MW; C822E342B8BEFF21 CRC64; MAVYRCGKCW KTFTDEQLKV LPGVRCPYCG YKIIFMVRKP TIKIVKAI //