ID   RPO12_METAC             Reviewed;          45 AA.
AC   P61933; Q8TPX9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=MA_4672;
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00615}.
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; AE010299; AAM05180.1; -; Genomic_DNA.
DR   AlphaFoldDB; P61933; -.
DR   SMR; P61933; -.
DR   STRING; 188937.MA_4672; -.
DR   EnsemblBacteria; AAM05180; AAM05180; MA_4672.
DR   KEGG; mac:MA_4672; -.
DR   HOGENOM; CLU_179456_2_1_2; -.
DR   InParanoid; P61933; -.
DR   PhylomeDB; P61933; -.
DR   Proteomes; UP000002487; 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   Pfam; PF03604; DNA_RNApol_7kD; 1.
DR   SMART; SM00659; RPOLCX; 1.
DR   SUPFAM; SSF63393; SSF63393; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..45
FT                   /note="DNA-directed RNA polymerase subunit Rpo12"
FT                   /id="PRO_0000159757"
FT   BINDING         8
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00615"
SQ   SEQUENCE   45 AA;  5379 MW;  387E44D2140D7653 CRC64;
     MGYKCTRCKQ KVEIDYEYTG IRCPYCGHRI LVKERPTTIK RIKAE