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RPO2C_METTH
ID   RPO2C_METTH             Reviewed;         603 AA.
AC   O27124;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=DNA-directed RNA polymerase subunit Rpo2C {ECO:0000305};
DE            EC=2.7.7.6 {ECO:0000250|UniProtKB:P11513};
DE   AltName: Full=DNA-directed RNA polymerase subunit B' {ECO:0000303|PubMed:9371463};
GN   Name=rpo2C {ECO:0000305}; Synonyms=rpoB1; OrderedLocusNames=MTH_1050;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
CC   -!- FUNCTION: DNA-dependent RNA polymerase (RNAP) catalyzes the
CC       transcription of DNA into RNA using the four ribonucleoside
CC       triphosphates as substrates. The Rpo2 subunit (Rpo2N and Rpo2C in this
CC       organism) is implicated in DNA promoter recognition and in nucleotide
CC       binding. {ECO:0000250|UniProtKB:B8YB55}.
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:0000250|UniProtKB:P11513};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:B8YB55};
CC       Note=Binds 1 Zn(2+) per subunit. {ECO:0000250|UniProtKB:B8YB55};
CC   -!- SUBUNIT: Part of the RNA polymerase complex.
CC       {ECO:0000250|UniProtKB:B8YB55}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:B8YB55}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC       {ECO:0000305}.
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DR   EMBL; AE000666; AAB85541.1; -; Genomic_DNA.
DR   PIR; F69006; F69006.
DR   RefSeq; WP_010876676.1; NC_000916.1.
DR   AlphaFoldDB; O27124; -.
DR   SMR; O27124; -.
DR   STRING; 187420.MTH_1050; -.
DR   EnsemblBacteria; AAB85541; AAB85541; MTH_1050.
DR   GeneID; 1471458; -.
DR   KEGG; mth:MTH_1050; -.
DR   PATRIC; fig|187420.15.peg.1029; -.
DR   HOGENOM; CLU_000524_2_2_2; -.
DR   OMA; YQKLYHM; -.
DR   Proteomes; UP000005223; 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:UniProtKB-KW.
DR   GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd00653; RNA_pol_B_RPB2; 1.
DR   Gene3D; 2.40.270.10; -; 1.
DR   Gene3D; 2.40.50.150; -; 1.
DR   InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR   InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR   InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR   InterPro; IPR007121; RNA_pol_bsu_CS.
DR   InterPro; IPR007646; RNA_pol_Rpb2_4.
DR   InterPro; IPR007647; RNA_pol_Rpb2_5.
DR   InterPro; IPR007641; RNA_pol_Rpb2_7.
DR   InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR   InterPro; IPR019969; RNAP_Rpo2.
DR   PANTHER; PTHR20856; PTHR20856; 1.
DR   Pfam; PF04566; RNA_pol_Rpb2_4; 1.
DR   Pfam; PF04567; RNA_pol_Rpb2_5; 1.
DR   Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR   Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR   TIGRFAMs; TIGR03670; rpoB_arch; 1.
DR   PROSITE; PS01166; RNA_POL_BETA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..603
FT                   /note="DNA-directed RNA polymerase subunit Rpo2C"
FT                   /id="PRO_0000048103"
FT   BINDING         546
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B8YB55"
FT   BINDING         549
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B8YB55"
FT   BINDING         564
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:B8YB55"
FT   BINDING         567
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   603 AA;  67687 MW;  17F2C0FC70BD5BBC CRC64;
     MSKTKIYING KLIGTCENPE EFVEEMRKKR RSGEVSPEMN ITHYPENHEI YIFTDPGRAR
     RPLIIVEDGE PLLTEEHLEK LETGEMSWDD LIAAGIIEYL DAEEEENAYI AMSPDEINDE
     HTHLEIDPST MLGICAGIIP FANHNSSPRN TMEAGMTKQA LGLYASNYDL RTDTRAHLLH
     HPQVPIVKTR IIDVTGYDER PSGQNFVVAV MSYEGYNMED ALILNKASLE RGLARSSFFR
     SYEAAERRYP GGQEDRFEIP EKGVRGYRSE SDYRHLDEDG IINPEAEVSS GDVLIGKTSP
     PRFLEEIDEF GTVAERRRET SVTVRHGEKG IVDAVLLTET VEGSRLAKIR VREQRQPELG
     DKFASRHGQK GVVGLIVSQE DMPFTEDGIV PDLIVNPHAI PSRMSVGQVL EMLAGKAACM
     EGRRVDGTPF TGEDEDDIKE ALRANGFETA GVESLYNGIT GERIEAEIFI GVAYYQKLHH
     MTTDKVYARS RGPVQVLTRQ PTEGRAREGG LRFGEMERDC LIAHGAALAL KERLLDESDK
     YEALVCADCG MIAVYDKIRD KKYCPICEDS ESFPVEVSYA FKLLLDELKS LCIFPKLILE
     DKA
 
 
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