RPOC_LISGR
ID RPOC_LISGR Reviewed; 1053 AA.
AC P77882;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, 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};
DE Flags: Fragment;
GN Name=rpoC {ECO:0000255|HAMAP-Rule:MF_01322};
OS Listeria grayi (Listeria murrayi).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1641;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25401 / DSM 20596 / CIP 76124 / NCTC 10812 / NRRL B-33018 /
RC F-9;
RA Morse R., Collins M.D., Balsdon J.T., Reading S., Richardson P.T.;
RT "Cloning part of the rpoC gene encoding the B' subunit of the DNA-dependent
RT RNA polymerase from some Gram-positive bacteria and comparative amino acid
RT sequence.";
RL Submitted (AUG-1996) 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; X89228; CAA61512.1; -; Genomic_DNA.
DR PIR; T09645; T09645.
DR AlphaFoldDB; P77882; -.
DR SMR; P77882; -.
DR PRIDE; P77882; -.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
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; 1.
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..>1053
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067755"
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"
FT NON_TER 1053
SQ SEQUENCE 1053 AA; 118564 MW; 75EF1CA24B83A857 CRC64;
MLDVNNFEYM KIGLASPDKI RSWSHGEVKK PETINYRTLK PERDGLFCER IFGPMKDWEC
SCGKYKRVRY KGVVCDRCGV EVTKSKVRRE RMGHIELAAP VSHIWYFKGI PSRMGLVMDM
SPRALEEIIY FASYVVTEPG DTPLEKKQLL SEKEYRVYRE KYGKNFHAGM GAEAIKKILS
DIDLEKETQE LKAELQTAQG QRRTRAIRRL EVMEAFRNSG NEPSWMILDV LPVIPPEIRP
MVQLEGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPNII VQNEKRMLQE AVDALIDNGR
RGRPVTGPGN RPLKSLSHML KGKQGRFRQN LLGKRVDYSG RSVIVVGPNL KMYQCGLPKE
MALELFKPFI MKELVSRGLA HNIKSAKRKI ERMAAEVWDV LEEVIREHPV LLNRAPTLHR
LGIQAFEPTL VEGRAIRLHP LVCTAYNADF DGDQMAVHVP LSAEAQAEAR LLMLAAQNIL
NPKDGKPVVT PSQDMVLGNY YLTLERENAV GEGLVFKDIN EAMIAYTNGY VHLHSRIGVY
AGSIQNERFT EEQRKQLLIT TVGKLVFNTI LPESFPYINE PTKYNLEIET PTKYFVDTTT
DVKTHIANQP LIDPFKKGIL GNIIAEVFKK FHITETSKML DRMKDLGFKI STKAGITVGI
ADILTLQEKP EILEKAHDKV EKITKQFRRG LITGDERYER VIGVWNAAKD EIQNKLILSL
ERLNPIFMMQ DSGARGNISN FTQLAGMRGL MADPSGRIVE LPITSNFREG LTVLEYFIST
HGARKGLTDT ALKTADSGYL TRRLVDVAQD VIIREDDCGT DRGLTIKAIR EGTEIIEPLE
ERLEGRYARK TIRHPETNEI IVKENDLITE DIAVQIIGAG IEEVSIRSAF TCNTKHGVCK
KCYGKNLATG TEVEVGEAVG IIAAQSIGEP GTQLTMRTFH TGGVAGDDIT QGLPRIQEIF
EARNPKGQAT ITEVAGEVVS IEEGRDRGLE ITIQGVDDRR SYTVPYTARL RVEVGSMLDR
GEALTEGSID PKALIRVRDV LSVQEYLLAE VQK
