RPO12_METJA
ID RPO12_METJA Reviewed; 46 AA.
AC P59283;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 1.
DT 03-AUG-2022, entry version 74.
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, ECO:0000303|PubMed:11058130};
DE Short=mjP {ECO:0000303|PubMed:11058130};
GN Name=rpo12 {ECO:0000255|HAMAP-Rule:MF_00615};
GN Synonyms=rpoP {ECO:0000255|HAMAP-Rule:MF_00615};
GN OrderedLocusNames=MJ0593.1;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP INTERACTION WITH RPO3, AND SUBUNIT.
RX PubMed=11058130; DOI=10.1093/nar/28.21.4299;
RA Werner F., Eloranta J.J., Weinzierl R.O.;
RT "Archaeal RNA polymerase subunits F and P are bona fide homologs of
RT eukaryotic RPB4 and RPB12.";
RL Nucleic Acids Res. 28:4299-4305(2000).
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 Note=Binds 1 zinc ion. {ECO:0000255|HAMAP-Rule:MF_00615};
CC -!- SUBUNIT: Part of the RNA polymerase complex (By similarity). Interacts
CC with Rpo3. Forms an Rpo3-Rpo10-Rpo11-Rpo12 complex upon coexpression
CC (PubMed:11058130). {ECO:0000255|HAMAP-Rule:MF_00615,
CC ECO:0000269|PubMed:11058130}.
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; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_064496553.1; NC_000909.1.
DR AlphaFoldDB; P59283; -.
DR SMR; P59283; -.
DR GeneID; 27929961; -.
DR InParanoid; P59283; -.
DR OrthoDB; 129924at2157; -.
DR PhylomeDB; P59283; -.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
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 Cytoplasm; DNA-directed RNA polymerase; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..46
FT /note="DNA-directed RNA polymerase subunit Rpo12"
FT /id="PRO_0000159758"
FT BINDING 9
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
FT BINDING 27
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
SQ SEQUENCE 46 AA; 5452 MW; 6B66BC918364EFA0 CRC64;
MVEYKCLNCK KIIKLEELGK RARCPHCSYK ILVKLRPKVV KHVKAR
