ID   RPOC_PARD8              Reviewed;        1431 AA.
AC   A6LE80;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
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=BDI_2263;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR43994.1; -; Genomic_DNA.
DR   RefSeq; WP_011966795.1; NC_009615.1.
DR   AlphaFoldDB; A6LE80; -.
DR   SMR; A6LE80; -.
DR   STRING; 435591.BDI_2263; -.
DR   PRIDE; A6LE80; -.
DR   EnsemblBacteria; ABR43994; ABR43994; BDI_2263.
DR   KEGG; pdi:BDI_2263; -.
DR   PATRIC; fig|435591.13.peg.2248; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_10; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   BioCyc; PDIS435591:G1G5A-2326-MON; -.
DR   Proteomes; UP000000566; 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   3: Inferred from homology;
KW   DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW   Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..1431
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000308871"
FT   BINDING         66
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         68
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         81
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         470
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         472
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         474
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         813
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         887
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         894
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         897
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1431 AA;  159784 MW;  EDEC7C7B156056D7 CRC64;
     MAFRKENKIK SNFSKITIGL ASPEEILENS SGEVLKPETI NYRTYKPERD GLFCERIFGP
     IKDYECHCGK YKRIRYKGIV CDRCGVEVTE KKVRRERMGH IHLVVPVAHI WYFRSLPNKI
     GYLLGLPTKK LDSIIYYERY VVIQPGCVDT VGELDLLSEE EYLDILDSLP RENQLLEDTD
     PNKFIAKIGA EAVYDLLARL DLDSLSYELR HRANTDTSQQ RKNEALKRLQ VVESFRASRG
     RNKPEWMIMK VIPVIPPELR PLVPLDGGRF ATSDLNDLYR RVIIRNNRLK RLIDIKAPEV
     ILRNEKRMLQ EAVDSLFDNS RKSSAVKTDA NRPLKSLSDS LKGKQGRFRQ NLLGKRVDYS
     ARSVIVVGPE LKMHECGLPK NMAAELYKPF VIRKLIECGI VKTVKSAKKI VDRKEPVVWD
     ILEYVMKGHP VLLNRAPTLH RLGIQAFQPK LIEGKAIQLH PLACTAFNAD FDGDQMAVHL
     PLGNEAVLEA QMLMLASHNI LNPANGAPIT VPSQDMVLGL YYITKLRKGT QGEGLTFYGP
     EEATIAYNEK KLDIHAPIHV YVEDLDENGN LVKTMVETSV GRLMVNEFVP KEIGYVNEVL
     GKKSLRDIIG RVIKACGVAR TAQFLDDIKN LGYYMAFKGG LSFNLADVLI PPEKDELVQK
     GYDEVEQIMA NYNMGFITNN ERYNQIIDTW THVNSNLSNI LIKQLTADND GFNSIYMMMD
     SGARGSKEQI RQLSGMRGLM AKPQKSGAEG GQIIENPILS NFKEGLSVLE YFISTHGARK
     GLADTALKTA DAGYLTRRLV DVSHDVIVNE EDCGTLRGLV CTELKNNEEV IASLYERILG
     RVSVHDVIHP ITGEVIVRSG EEIREDAAKA IQDSPIESVE IRSVLTCESK KGVCAKCYGR
     NLATNRMVQK GEVVGVIAAQ SIGEPGTQLT LRTFHVGGIA SNIATENSIT SKYDGILEID
     ELRAVEAVDE VSGKKHLVVV SRLAEMRIVD PNTKIVLLTH NIPYGSKLFF NNGDSIKKGD
     VIIEWDPFNA VIVSEVSGKI EFESLVENVT YKVESDETTG LKEKIIIESK DKTKAPAAHI
     VDENGNYLKN YSLPLGAHVV KDNGDVVKAG EVLVKIPRAV GKAGDITGGL PRVTELFEAR
     NPSNPAVVSE IDGEVGFGKI KRGNREITVT SKLGEVKKYM VPLSKQLLVQ ENDYIRAGMP
     LSDGATTPSD ILAIKGPTAV QEYIVNEVQD VYRLQGVKIN DKHFEVIVRQ MMRKVEVVDP
     GDTRFLEQQI VDKLEVMDEN DRIWGKKVVT DPGDSQTLQA GQIVTARKLR DENSMLKRRD
     LKLVEVRDAI PATANQILQG ITRAALQTNS FMSAASFQET TKVLNEAAIN GKVDRLEGLK
     ENVICGHLIP AGTGQREFDK LIVGAKDEFD RIFANRKNVV DFNAMDKDDE E