RPOC_PASMU
ID RPOC_PASMU Reviewed; 1417 AA.
AC Q9CK92;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=PM1736;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03820.1; -; Genomic_DNA.
DR RefSeq; WP_005724687.1; NC_002663.1.
DR AlphaFoldDB; Q9CK92; -.
DR SMR; Q9CK92; -.
DR STRING; 747.DR93_618; -.
DR PRIDE; Q9CK92; -.
DR EnsemblBacteria; AAK03820; AAK03820; PM1736.
DR KEGG; pmu:PM1736; -.
DR PATRIC; fig|272843.6.peg.1758; -.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000809; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1417
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067772"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 89
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 896
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"
SQ SEQUENCE 1417 AA; 157187 MW; 9F717538EDF1F140 CRC64;
MKDLVKFLKA QSKTSEDFDV IKIGLASPDM IRSWSFGEVK KPETINYRTF KPERDGLFCA
RIFGPVKDYE CLCGKYKRLK HRGVICEKCG VEVTQTKVRR ERMGHIELAS PVAHIWFLKS
LPSRIGLLLD MPLRDIERVL YFESYIVIEP GMTDLDKGQL LTEEQYIDAE DRWGDEFDAK
MGAEAIQALL RDMDLPQECE NLREELQETN SETKRKKITK RLKLLEAFIQ SGNKPEWMVM
TVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLDLIAPD IIVRNEKRML
QESVDALLDN GRRGRAITGS NRRPLKSLAD MIKGKQGRFR QNLLGKRVDY SGRSVITVGP
YLHLHQCGLP KKMALELFRP FIYAKLESRG FASTIKAAKK MVEREDAIVW DILADVIREH
PILLNRAPTL HRLGIQAFEP LLIEGKAIQL HPLVCAAFNA DFDGDQMAVH VPLTLEAQLE
ARALMMSTNN ILSPANGEPI IVPSQDVVLG LYYMTRDKVN GKGEGMLLQD PREAEKAYRT
GQVELHSRVK VRITEYVKNA VGEFEPQTNL VDTTIGRAIL WMIAPKGMPF SLFNQTLGKK
AISKLINESY RRLGMKPSVL FADQIMYTGF AYAARSGSSV GIDDMVIPAK KYEIISAAED
EVAEIQEQFQ SGLVTAGERY NKVIDIWAAA NERVAKAMME NLSTEEVINR EGQPEKQASF
NSIFMMADSG ARGSAAQIRQ LAGMRGLMAR PDGSIIETPI TANFREGLNV LQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVAQDLVI IEDDCGTHEG IVMTPLIEGG DVKEALRDRV
LGRVVAEDVL KPGTEEVLIA RNTLLDEKLC DVIDSNSVDS IKVRSVVTCN TDFGVCAKCY
GRDLARGHLI NQGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASAAAKESS IQVKNTGTLR
LANVKFVTNN EGKLVLTSRN TELTIIDAFG RTKEHYKVPY GAILSKGDGQ EVTAGETVAN
WDPHTMPVVS EVSGFVKFID LIDGLTVTRQ TDELTGLSSI VVQDVGERAT AGKDLRPAIK
LVDAKGNDIL IPGTDVVAQY FLPGKAIVTL DDNAEVHIGE PLARIPQESV GTKDITGGLP
RVADLFEARK PKEPAILAEI SGIVSFGKET KGKRRLLITP AEGETYEEMI PKWRQLNVFE
GEMVERGDLI SDGAETPHDI LRLRGVHAVT EYIVNEVQEV YRLQGVKIND KHIEVIVRQM
LRKGIVTKAY DSEFLEGEQV EVARVKIVNR KREAEGKPLV EFERELLGIT KASLATESFI
SAASFQETTR VLTEAAVAGK RDELRGLKEN VIVGRLIPAG TGFAYHQNRQ KKVVMSDEMP
VKLSAADEEE IAAEFTVTAE DATASLAEML NMADDAE
