RPOC_CLOD6
ID RPOC_CLOD6 Reviewed; 1161 AA.
AC Q18CF3;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=CD630_00670;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
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; AM180355; CAJ66882.1; -; Genomic_DNA.
DR RefSeq; WP_003429485.1; NZ_CP010905.2.
DR RefSeq; YP_001086531.1; NC_009089.1.
DR PDB; 7L7B; EM; 3.26 A; D=1-1161.
DR PDBsum; 7L7B; -.
DR AlphaFoldDB; Q18CF3; -.
DR SMR; Q18CF3; -.
DR STRING; 272563.CD630_00670; -.
DR ChEMBL; CHEMBL2363852; -.
DR DrugCentral; Q18CF3; -.
DR PRIDE; Q18CF3; -.
DR EnsemblBacteria; CAJ66882; CAJ66882; CD630_00670.
DR GeneID; 66352565; -.
DR KEGG; cdf:CD630_00670; -.
DR KEGG; pdc:CDIF630_00133; -.
DR PATRIC; fig|272563.120.peg.73; -.
DR eggNOG; COG0086; Bacteria.
DR OMA; YRNIRVE; -.
DR PhylomeDB; Q18CF3; -.
DR BioCyc; PDIF272563:G12WB-121-MON; -.
DR PRO; PR:Q18CF3; -.
DR Proteomes; UP000001978; 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; -; 2.
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 1: Evidence at protein level;
KW 3D-structure; DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1161
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353335"
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 790
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 864
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 874
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1161 AA; 129729 MW; 5C530F496171DA22 CRC64;
MFELNNFESI KIALASPEKI RQWSRGEVKK PETINYRTLK PEKDGLFCER IFGPQKDWEC
HCGKYRRVRY KGVVCDRCGV EVTKSKVRRE RMGHIELAAP MSHIWYFKGI PSRMGLLLDM
SPRSLEKILY FASYVVVDPG ETGLNEKQLL TEKEYRTALE KYGYTFTVGM GAEAVKTLLQ
NIDLEQQSKD LRAELKDSTG QKKVRTIRRL EVVEAFKKSG NKPEWMILDA IPVIPPDLRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLKR LLELGAPDII VRNEKRMLQE AVDALIDNGR
RGRPVTGPGN RPLKSLSDML KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KFYQCGLPKK
MALELFKPFV MDKLVKEGYA HNIKSAKSIV EKVKPEVWDV LEDVIKSHPV LLNRAPTLHR
LGIQAFEPIL VEGKAIKLHP LVCTAYNADF DGDQMAVHVP LSVEAQAEAR FLMLSVNNIL
APKDGSPITT PSQDMVLGCY YLTIEAQDGA KGTGMVFKDF NELLLAYYNK SVHLHALVKL
KVTLEDGRSS LVESTVGRFI FNENIPQDLG FVDRKENPFA LEVDFLADKK SLGKIIDKCF
RKHGNTETAE LLDYIKALGF KYSTLGGITV AVDDMSVPEE KKVFIAEAEA KVDKYEKAYR
RGLISDEERY EKVIETWTET TDKVTDALMG GLDRLNNIYI MAHSGARGSK NQIRQLAGMR
GLMANASGKT VEIPVKSNFR EGLSVLEYFT SSHGARKGLA DTAIRTAESG YLTRRLVDVS
QDVIVREIDC GTEDTTEIYA IKEGNEVIEE IYDRIVGRYT IDPILNPETG EVIVEADSMI
QEDEAETIVA LGIEKIRIRT VLNCKTNHGV CSKCYGRNLA TGKEVNIGEA VGIIAAQSIG
EPGTQLTMRT FHTGGVAGAD ITQGLPRVEE LFEARKPKGL AVITEVSGRV EIDETGKRKE
VNVIPEEGET QTYVIPYGSR LKVKQGQMLE AGDPLTQGFI NPHDIVRVNG VKGVQEYIVK
EVQRVYRLQG VDVNDKHIEV IVRQMLSKVK VEDPGDTDLL PGGYEDVLTF NECNKDAIDK
GLRPAVAKRV LLGITKASLA TDSFLSAASF QETTRVLTEA AIKGKEDHLI GLKENVILGK
LIPAGTGMKK YRNIAVEKIE D
