RPOC_GEOTN
ID RPOC_GEOTN Reviewed; 1199 AA.
AC A4IJI2;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE Short=RNAP subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=RNA polymerase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
DE AltName: Full=Transcriptase subunit beta' {ECO:0000255|HAMAP-Rule:MF_01322};
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322}; OrderedLocusNames=GTNG_0099;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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_01322};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01322};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01322};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01322};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
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DR EMBL; CP000557; ABO65486.1; -; Genomic_DNA.
DR RefSeq; WP_029761768.1; NC_009328.1.
DR AlphaFoldDB; A4IJI2; -.
DR SMR; A4IJI2; -.
DR STRING; 420246.GTNG_0099; -.
DR PRIDE; A4IJI2; -.
DR EnsemblBacteria; ABO65486; ABO65486; GTNG_0099.
DR KEGG; gtn:GTNG_0099; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_9; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; 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 Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR045867; DNA-dir_RpoC_beta_prime.
DR InterPro; IPR012754; DNA-dir_RpoC_beta_prime_bact.
DR InterPro; IPR000722; RNA_pol_asu.
DR InterPro; IPR006592; RNA_pol_N.
DR InterPro; IPR007080; RNA_pol_Rpb1_1.
DR InterPro; IPR007066; RNA_pol_Rpb1_3.
DR InterPro; IPR042102; RNA_pol_Rpb1_3_sf.
DR InterPro; IPR007083; RNA_pol_Rpb1_4.
DR InterPro; IPR007081; RNA_pol_Rpb1_5.
DR InterPro; IPR044893; RNA_pol_Rpb1_clamp_domain.
DR InterPro; IPR038120; Rpb1_funnel_sf.
DR PANTHER; PTHR19376; PTHR19376; 1.
DR Pfam; PF04997; RNA_pol_Rpb1_1; 1.
DR Pfam; PF00623; RNA_pol_Rpb1_2; 2.
DR Pfam; PF04983; RNA_pol_Rpb1_3; 1.
DR Pfam; PF05000; RNA_pol_Rpb1_4; 1.
DR Pfam; PF04998; RNA_pol_Rpb1_5; 2.
DR SMART; SM00663; RPOLA_N; 1.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1199
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353373"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 818
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 902
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1199 AA; 134807 MW; 012E17A7A775BC16 CRC64;
MLDVNKFEYM KIGLASPEKI RSWSYGEVKK PETINYRTLK PEKDGLFCER IFGPTKDWEC
HCGKYKRVRY KGVVCDRCGV EVTRSKVRRE RMGHIELAAP VSHIWYFKGI PSRMGLVLDM
SPRALEEVIY FASYVVTDPG DTPLEKKQLL SEKEYRAYRE KYGQSFQASM GAEAIKKLLQ
DIDLDKEVAT LKEELKTAQG QRRARIIKRL EVLESFRSSG NDPAWMVLDV LPVIPPELRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPNII VQNEKRMLQE AVDALIDNGR
RGRPVTGPGN RPLKSLSHML KGKQGRFRQN LLGKRVDYSG RSVIVVGPNL KMYQCGLPKE
MALELFKPFV MKELVERGLA HNIKSAKRKI ERVHPEVWDV LEDVIKEHPV LLNRAPTLHR
LGIQAFEPTL VEGRAIRLHP LVCTAYNADF DGDQMAVHVP LSAEAQAEAR LLMLAAQNIL
NPKDGKPVVT PSQDMVLGNY YLTMEREGAI GEGMVFKDTD EALLAYHNGY VHLHSRIAIH
AGSLKNETFT PEQNNKLLLT TVGKLIFNEI LPKSFPYINE PTTENIEGRT PDKYFLDKGV
DVREEIRKRE LVPPFKKKVL GQIIAEVFKR FKITETSKML DRMKDLGFQY STKAGITIGV
SDIVVLPEKQ EILDEAQAKV DTVLKQFRRG LITDEERYER VISVWSAAKD KIQDRLMKSL
DKRNPIFMMS DSGARGNASN FTQLAGMRGL MANPAGRIIE LPIKSSFREG LTVLEYFIST
HGARKGLADT ALKTADSGYL TRRLVDVAQD VIVREEDCGT DRGILARALT DGTEVVVKLE
ERLVGRYAHK TVHHPETGEV IVRKDEMITE DIANEIIKAG ITEVWIRSVF ACNTRHGVCK
KCYGRNMATG MDVEVGEAVG IIAAQSIGEP GTQLTMRTFH TGGVAGDDIT QGLPRVQELF
EARNPKGQAV ISEIDGTVVA INETRDNQYE IVVQSEVETR SYVAPYNARL KVEEGQHVER
GQELTEGSVD PKQLLRVRDI TSVQEYLLRE VQKVYRMQGV EISDKHIEVM VRQMLRKVRV
IDAGDTDVLP GTLLDVHQFT DVNAQAIREG KRPATARPVL LGITKASLET DSFLSAASFQ
ETTRVLTDAA IKGKRDELLG LKENVIIGKL VPAGTGMARY RNVKPAVKKE TASDTVPSN
