RPOC_PEDAC
ID RPOC_PEDAC Reviewed; 1055 AA.
AC P77917;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 84.
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 Pediococcus acidilactici.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Pediococcus; Pediococcus acidilactici group.
OX NCBI_TaxID=1254;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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, ECO:0000305}.
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DR EMBL; X89232; CAA61516.1; -; Genomic_DNA.
DR PIR; T10432; T10432.
DR AlphaFoldDB; P77917; -.
DR SMR; P77917; -.
DR STRING; 1254.A4V11_04575; -.
DR PRIDE; P77917; -.
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..>1055
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067773"
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 1055
SQ SEQUENCE 1055 AA; 117925 MW; FE1BDDB4C6C6B582 CRC64;
MIDVNKFESM QIGLASPDKI RMWSYGEVKK PETINYRTLK PEKDGLFDER IFGPTKDYEC
ACGKYKRIRY KGIVCDRCGV EVTKSKVRRE RMGHIELAAP VTHIWYFKGI PSRMGLVLDM
SPRSLEEIIY FASYVVVDPG DTPLEKKQLL TEREYRAKLD EYGNRFVAKI GGEAIQALLQ
SVDLEKEANL LKEELKEASG QKRTRAVRRL DIIEAFIKSG NHPDWMVMDA IPVMPPDLRP
MVQLDGGRFA TSDLKHLYRR VINRNNRLKR LLDLNAPGII VQNEKRMLQE AVDALIDNGR
RGRPVAGPGN RPLKSLSHML KGKQEGFRQN LLGKRVDYSG RSVIDVGPSL KMNQMGLPVP
MAMELFKPFI MKELVSRNLA SNIKNAKRKI DRKDEEVYDV LEDVIKEHPV LLNRAPTLHR
LGIQAFEPVL VSGKAMRLHP LACEAYNADF DGDQMAIHVP LSNEAQAEAR LLMLAAHHIL
APKDGKPVVT PSQDMVIGNY WLTMERAESV GEGMIFNDLD EVKLALQNGY VSIHTRIGVR
ASSMPEKPFT DQQRQQILIT TAGKMLFNDI LPKDFVYLNA PTNEKLVNGT PDEYFLEAGE
DIHEQLNQRP LLSPFKSGFL SDVIAEVYKQ YKVTETSLLL DRMKDLGFYR STLSGLTVGI
ADITNLPDKP AIIAAAHKKV ATVTKQFRRG LITDDERYER VIGIWNDAKD EIQQRLMDTF
DPQNPIFMMS DSGARGNISN FTQLAGMRGL MAAPNGKIME LPILSNFREG LSVLEMFIST
HGARKGMTDT ALKTANSGYL TRRLVDVAQD VIVREKDCGT DRGLLITAIA EGNEMIEPLY
DRILGRYTMK SVINPETGKV IVGQNEMIDE RSAQEIIDAG IQEVTIRSAF TCNTAHGVCE
KCYGRNMATG DRVEVGEAVG TVAAQSIGEP GTQLTMRNFH TGGVAGNADI TQGLPRIQEI
VEARNPKGPA EISEVTGVVE SIEEDPAEGT KEVTVKGETD SRTYSLPITA RMKVAEGDYI
HRGAPLNEGS IDPKKLIKVR DVLSTENYLL SEIQK
