RPOC_BROTH
ID RPOC_BROTH Reviewed; 1053 AA.
AC P77839;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 78.
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 Brochothrix thermosphacta (Microbacterium thermosphactum).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Brochothrix.
OX NCBI_TaxID=2756;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCDO 1676;
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 1 Zn(2+) ion per subunit. {ECO:0000255|HAMAP-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, ECO:0000305}.
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DR EMBL; X89231; CAA61515.1; -; Genomic_DNA.
DR AlphaFoldDB; P77839; -.
DR SMR; P77839; -.
DR STRING; 2756.BFR44_11410; -.
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; 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..>1053
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067719"
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 NON_TER 1053
SQ SEQUENCE 1053 AA; 118003 MW; 9CA0172887929825 CRC64;
MLDVNNFEYM KIGLASPDKI RSWSFGEVKK PETINYRTLK PERDGLFCER IFGPTKDWEC
SCGKYKRVRY KGVVCDRCGV EVTKSKVRRE RMGHIELAAP VSHIWYFKGI PSRMGLVLDM
SPRALEEVIY FASYVVTEAG DTALDKKQLL SEREYRAYRE KYGQSFQAGM GAEAIKRLLD
AVDLEGEVTE LKEELKSAQG QRRTRAIRRL EVLEAFRHSG NKPSWMVLDV LPVIPPEIRP
MVQLEGGRFA TSDLNDLYRR VINRNNRLKR LLDLGAPSII VQNEKRMLQE AVDGLIDNGR
RGRPVTGPGN RPLKSLSHML KGKQGRFRQN LLGKRVDYSG RSVIVCGPSL KMYQCGLPRE
MAIELFKPFV MRELTQRGLA HNIKSAKRKI ERHSPEIWDV LEDVIREHPV LLNRAPTLHR
LGIQAFEPIL VEGRAIRLHP LVCTAYNADF DGDQMAVHVP LSPEAQAEAR ILMLAANHIL
NPKDGKPVVT PSQDMVLGNY YLTLERENIV GEGLVFTDIN EAMIAYQNGY VHLHSRVAVA
AASLGNETFT AEQNNQLLIT TVGKMIFNSI LPPSFPYLNE PTKTNLEVAT PSQYFVPTTT
DVKAHIEKQA FLLPFKKKNL EEIIAQIFKL FHITETSKML DRMKDQGFKY STLAGITVGI
SDIIVVKDKP EILAASHDEV DNVTKMFKRG LMTDEERYER VIAIWNAAKD QLQNKLIAGL
DRLNPIFMMQ DSGARGNISN FTQLAGMRGL MADPSGRIVE LPITSNFREG LNVLEYFISS
HGARKGLTDT ALKTADSGYL TRRLVDVAQD VIVRETNDGS DHGLLVSDIV EGPEVIETLT
ERLEGRYSAK TVRHPETNEV MIRPDELFTQ EIAEAIPAAG IKEVWIRSVF TCNTKHGVSK
ISYGKDLSTG SEVEVGEAVG IVAAQSIGEP GTQLTMRTFH TGGVAGSDIT QGLPRIQEIF
EARNPKGHAV ITELTGEVKA IEEKANRQRE ITVTGTQETR TYTVPMVARL KVKVGDAVRR
GDPLMDGSID PKELLHVTDV ITVENYLLGE VQK
