RPOC_MYCCT
ID RPOC_MYCCT Reviewed; 1255 AA.
AC Q2ST47;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=MCAP_0071;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000123; ABC01241.1; -; Genomic_DNA.
DR RefSeq; WP_011386971.1; NC_007633.1.
DR AlphaFoldDB; Q2ST47; -.
DR SMR; Q2ST47; -.
DR EnsemblBacteria; ABC01241; ABC01241; MCAP_0071.
DR GeneID; 23778974; -.
DR KEGG; mcp:MCAP_0071; -.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR PhylomeDB; Q2ST47; -.
DR Proteomes; UP000001928; 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; 1.
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..1255
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240809"
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 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 875
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 950
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 957
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 960
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1255 AA; 141318 MW; D58BABC59AC473E9 CRC64;
MENLNRKKAI KIELANPDTI RSWSHGEVLK PETINYKTLK AEKDGLFDER IFGPTKNYEC
VCGRYKKANP MNKGKKCEKC GVELTESIVR RERMGHIELE EPVTHIWMLK VAPYRIAAIL
DLKAKELEEV VYFVSHIVLE QGNQSHFLEK EVLDLGSSRI TKTREKLQLS ILDVIDQIND
PEHRDTKKAN RLLEELKNTS IPFSIDEATS LISKYTNAKF GIGARAVEYL LEKVDLTKEI
EAIKIQLENS KKTPNERTKL LKRLETFDSL KRSKQRPEWM VMRVIPVIPP DIRPIIQLDG
GRFTTSEIND LYRRIIIRNE RLKKVKEMGA PSIIVNNEKR MLQEAVDALF DNERKPKPVQ
GKNKRPLKSL TSVLKGKQGR FRQNLLGKRV DYSARSVIAI GPDLKMYQAG LPREMAITLF
KPFVIQWLQD HEYAENVKIA EKMLLQNDPK VWEALEQVIK DRPVLLNRAP TLHRLGIQAF
EPKLVKGKAI RLHPLVTTAF NADFDGDQMA VHVPITKEAV AESRALMLGS SAILGPKDGK
AIVTPGQDII LGNYYLTTEE KNAKGQGMIF SSLDEAFMAY NSGQIHLNSL IGIALSALPE
EKFSDKNQRL NSYLLTTVGK LYFNQIFDDN FPWINSNNIW NAKEAVKEFI YDFSQDIDKV
IENVQVQQPI KKKELSLIIE RYFETHGARK TAEMLDKMKD LGFSFSTKSG TTISAGDVVA
FTHKYDEFKE ADQKVEQITD FYNMGMLTNS EKKRRIIDVW SEVKDKIQNE LATVLRKDVK
NPIFVMVDSG ARGNVSNFTQ LVGMRGLMND TKGDIKEIPI KSSFREGLTV SEYFVSTHGA
RKGMADIALK TADSGYLTRR LVDVSQEIVV VNEDCEPTKG FEVSAIIDTK HDNVIVPLKD
RLVGRFTFED IYDDDKNLVA SANTLIDKNI AEKIIMSGIS SVIIRSVLTC DNKRGVCQKC
YGLNLATASV VNIGEPVGVI AAQSIGEPGT QLTMRNFHTG GVAGNVDITQ GLPRIKELLD
VTTPKGAVAI ISEVDGVVSE IEDYNGVFVI NIVTENEEVK KYKTEFNSVL RVEQGSSVMA
GQKLTEGAID LHQLLEFGGI QDVQNYILKE VQKVYRLQGI EISDKYIEII IKQMLNKVKI
TDSGDSDLLP GEIITIQNYK EVVQDCIVKS IRPPLSKAQI FGIKKAPLES SSWLSSASFQ
DTARVLTRAI IKGKEDKLEG LKENIMLGNL IPAGTGLTGT QEVEQLAEQY HNNEY
