RPO2C_METTW
ID RPO2C_METTW Reviewed; 604 AA.
AC P09845; P72014;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 94.
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:2834336};
GN Name=rpo2C {ECO:0000305}; Synonyms=rpoB1, rpoU;
OS Methanothermobacter thermautotrophicus (strain Winter) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79930;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2843811; DOI=10.1093/nar/16.16.8113;
RA Berghoefer B., Kroeckel L., Koertner C., Truss M., Schallenberg J.,
RA Klein A.;
RT "Relatedness of archaebacterial RNA polymerase core subunits to their
RT eubacterial and eukaryotic equivalents.";
RL Nucleic Acids Res. 16:8113-8128(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-55.
RX PubMed=2834336; DOI=10.1128/jb.170.5.2247-2253.1988;
RA Schallenberg J., Moes M., Truss M., Reiser W., Thomm M., Stetter K.O.,
RA Klein A.;
RT "Cloning and physical mapping of RNA polymerase genes from Methanobacterium
RT thermoautotrophicum and comparison of homologies and gene orders with those
RT of RNA polymerase genes from other methanogenic archaebacteria.";
RL J. Bacteriol. 170:2247-2253(1988).
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; X08038; CAA30837.1; -; Genomic_DNA.
DR EMBL; M20391; AAA72653.1; -; Genomic_DNA.
DR PIR; S02195; S02195.
DR AlphaFoldDB; P09845; -.
DR SMR; P09845; -.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..604
FT /note="DNA-directed RNA polymerase subunit Rpo2C"
FT /id="PRO_0000048104"
FT ACT_SITE 348
FT /evidence="ECO:0000250"
FT ACT_SITE 481
FT /evidence="ECO:0000250"
FT BINDING 547
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 550
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 565
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
SQ SEQUENCE 604 AA; 68114 MW; 97177D1F9E15A23D CRC64;
MNKTKIYING KLIGTCDNPE EFVEEIRAKR RSGEVSHEMN ITHYPENHEI YIFTDPGRAR
RPLIIVEDGE PLLKEEHLEK LSSGEMEWDD LISQGIIEYL DAEEEENTYI AMSPEEVTEE
HTHLEIDPST MLGICAGIIP FANHNSSPRN TMEAGMTKQA LGLYASNYNL RTDTRAHLLH
HPQVPIVKTR IIDVTGYDER PSGQNFVVAV MSYEGYNMED ALILNKASLE RGLARSSFFR
SYEATERRYP GGQEDRFEIP EKGVRGYRSE RDYRHLDEDG IINPETEVSS GDVLIGKTSP
PRFLEEIDEF GTVAERRRET SVTVRHGEEG IVDAVLLTET VEGSRLAKIR VREQRQPEFI
GDKFASRHGQ KGVVGLIVSQ EDMPFTEDGV VPDLIVNPHA IPSRMSVGQV LEMLAGKAAC
MEGRRVDGTP FTGEEEKDLK EALKANGFES AGVETLYNGI TGERIEAEIF IGVAYYQKLH
HMTTDRIYAR SRGPVQVLTR QPTEGRAREG GLRFGEMERD CLIAHGAALA LKERLLDESD
KYEALVCAEC GMIAIYDKIR DKKYCPICED SESFPVEISY AFKLLLDELK SLCIFPKLVL
EDKA
