RPOC_MANSM
ID RPOC_MANSM Reviewed; 1420 AA.
AC Q65W40;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 2.
DT 03-AUG-2022, entry version 91.
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=MS0213;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAU36820.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE016827; AAU36820.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041639466.1; NC_006300.1.
DR AlphaFoldDB; Q65W40; -.
DR SMR; Q65W40; -.
DR STRING; 221988.MS0213; -.
DR PRIDE; Q65W40; -.
DR EnsemblBacteria; AAU36820; AAU36820; MS0213.
DR KEGG; msu:MS0213; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000607; 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..1420
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225549"
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 1420 AA; 157562 MW; 666EA5FD2699B636 CRC64;
MKDLVKFLKA QSKTSEDFDV IKIGLASPDM IRSWSFGEVK KPETINYRTF KPERDGLFCA
RIFGPVKDYE CLCGKYKRLK HRGVICEKCG VEVTQTKVRR ERMGHIELAS PVAHIWFLKS
LPSRIGLLLD MPLRDIERVL YFESYIVIEP GMTDLEKGQL LTEEQFMDAE DRWADEFDAK
MGAEAIQALL RDMDLEHECE TLREELQETN SETKRKKITK RLKLLEAFMQ SGNKPEWMVM
TVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLDLVAPD IIVRNEKRML
QESVDALLDN GRRGRAITGS NKRPLKSLAD MIKGKQGRFR QNLLGKRVDY SGRSVITVGP
YLRLHQCGLP KKMALELFRP FIYAKLESRG FASTIKAAKK MVEREDAIVW DILAEVIREH
PILLNRAPTL HRLGIQAFEP ILIEGKAMQL HPLVCAAFNA DFDGDQMAVH VPLTLEAQLE
ARALMMSTNN VLSPANGDPI IVPSQDVVLG IYYMTREKVN AKGEGMLLQD PREAEKAYRT
GRAELHSRVK IRITEYVKNA EGEFEPQTTL TDTTIGRAIL WMIAPKGMPY SLFNQTLGKK
AISKLINECY RRLGVKASVM FADQIMYTGF AYAARSGSSV GIDDMVIPEK KYEIISAAEA
EVAEIQEQFQ SGLVTAGERY NKVIDIWATA NERVAKAMME NLSTEEVVNR EGNLEKQSSF
NSIFMMADSG ARGSAAQIRQ LAGMRGLMAR PDGSIIETPI TANFREGLNV LQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVAQDLVI VEDDCGTHEG IVMTPLIEGG DEKVSLRELV
LGRVAAEDIL KPGTEEVLFP RNTLLDEKVC DILDENSVDS VKVRSVVTCD TDFGVCAKCY
GRDLARGHLI NQGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASAAAKESS VQVKNSGSIR
LTNVKSVTNN EGKLVVTSRN TELTIIDAFG RTKEHYKVPY GAVLNKGDGE AVTAGETVAN
WDPHTMPVVS EVAGFVKFVD IVDGLTVTRQ TDELTGLSSI VVQDVGERAT AGKDLRPAIK
VVDAQGNDIF IPGVDVLAQY FLPGKAIVTL DDGAEVQVGE PLARIPQESV GTKDITGGLP
RVADLFEARK PKEPAILAEI TGIVSFGKET KGKRRLVITP VEGEAYEEMI PKWRQLNVFE
GEMVERGDVI SDGAETPHDI LRLRGVHAVT EYIVNEVQEV YRLQGVKIND KHIEVIVRQM
LRKGIITKAY DSEFLEGEQV EVARVKIVNR KREAEGKPPV EFERELLGIT KASLATESFI
SAASFQETTR VLTEAAVAGK RDELRGLKEN VIVGRLIPAG TGFAYHQNRI KNRGQANVVE
EQEVKFSAAD EAEIEAEFNM IAEDPAASLA EMLNMADDAE
