RPO12_SACS2
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 03-AUG-2022, entry version 103.
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}; OrderedLocusNames=SSO5865;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; 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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00615,
CC 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}.
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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 EnsemblBacteria; AAK40770; AAK40770; SSO5865.
DR GeneID; 7812440; -.
DR GeneID; 7940339; -.
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:transcription, DNA-templated; IEA:UniProtKB-UniRule.
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; SSF63393; 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
