RPO2C_METJA
ID RPO2C_METJA Reviewed; 636 AA.
AC Q60181;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
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:8688087};
GN Name=rpo2C {ECO:0000305}; Synonyms=rpoB1; OrderedLocusNames=MJ1041;
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).
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; L77117; AAB99044.1; -; Genomic_DNA.
DR PIR; H64429; H64429.
DR AlphaFoldDB; Q60181; -.
DR SMR; Q60181; -.
DR STRING; 243232.MJ_1041; -.
DR EnsemblBacteria; AAB99044; AAB99044; MJ_1041.
DR KEGG; mja:MJ_1041; -.
DR eggNOG; arCOG01762; Archaea.
DR HOGENOM; CLU_000524_2_2_2; -.
DR InParanoid; Q60181; -.
DR OMA; YQKLYHM; -.
DR PhylomeDB; Q60181; -.
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: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..636
FT /note="DNA-directed RNA polymerase subunit Rpo2C"
FT /id="PRO_0000048102"
FT BINDING 551
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 554
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:B8YB55"
FT BINDING 572
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000305"
SQ SEQUENCE 636 AA; 72193 MW; 81DE30267A572914 CRC64;
MKNLASREVN IYVNGKLVGT TDKPEELVNF IREKRRKGEL PQYTTVAYNE ESNDIHINTD
AGRIVRPLIV VENGKPKLTK EHIEKLKKGE ITFSDLVKEG VIEYLDAEEE ENAYIALSEE
ELTEKHTHLE IDPLTILGIG AGVAPYPEHN SAPRITMAAA MGKQSLGIPM SNIKWRLDTR
GHYLHYPQVP IVRTKHQEIL GFDKRPAGQN FVVAIMSYEG YNMEDAIVFN KSAIDRGLGR
STFFRTYDAC ERRYPGGQMD RFEIPDKGVR GYRSEECYRY LEEDGIVAVE SHVKGGDVIV
GKTSPPRFLE EHEITIQVKP QRRDSSVVVR HGEEGYIDKV ILTETKEGNR LVKVKVRDLR
IPELGDKFAS RHGQKGVMGL TVPQEDLPFT ESGIVPDIII NPHAIPSRMT VGQLLEMLGG
KVGALEGRRI DGTIFSGEKE WDLRKALEAL GFKHHGKEVM YDGKTGKKFE VEIYIGIAYY
QKLHHLVAGK IHARSRGPVQ VLTRQPTEGR AREGGLRFGE MERDVLIGHG AAMLLKERLM
DESDPYDICI CSKCGDFAIL DYKRGLKYCP ICGEIENLYS SKKIPFVRIP YAFKLLLDEL
KSMCILPRIK VRDKVELEDF EEFVEKLEKE KVKQKQ
