RPOC_BACTN
ID RPOC_BACTN Reviewed; 1427 AA.
AC Q8A470;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=BT_2733;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO77839.1; -; Genomic_DNA.
DR RefSeq; NP_811645.1; NC_004663.1.
DR RefSeq; WP_011108455.1; NC_004663.1.
DR AlphaFoldDB; Q8A470; -.
DR SMR; Q8A470; -.
DR STRING; 226186.BT_2733; -.
DR PaxDb; Q8A470; -.
DR PRIDE; Q8A470; -.
DR EnsemblBacteria; AAO77839; AAO77839; BT_2733.
DR KEGG; bth:BT_2733; -.
DR PATRIC; fig|226186.12.peg.2776; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR InParanoid; Q8A470; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000001414; 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; 2.
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..1427
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067708"
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 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 476
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 1427 AA; 158439 MW; 6604834F902AE02E CRC64;
MAFRKENKTK SNFSKISIGL ASPEEILENS SGEVLKPETI NYRTYKPERD GLFCERIFGP
IKDYECHCGK YKRIRYKGIV CDRCGVEVTE KKVRRERMGH IQLVVPVAHI WYFRSLPNKI
GYLLGLPTKK LDSIIYYERY VVIQPGVKAE DGIAEYDLLS EEEYLDILDT LPKDNQYLED
NDPNKFIAKM GAEAIYDLLA RLDLDALSYE LRHRAGNDAS QQRKNEALKR LQVVESFRAS
RGRNKPEWMI VRIVPVIPPE LRPLVPLDGG RFATSDLNDL YRRVIIRNNR LKRLIEIKAP
EVILRNEKRM LQESVDSLFD NSRKSSAVKT DANRPLKSLS DSLKGKQGRF RQNLLGKRVD
YSARSVIVVG PELKMGECGI PKLMAAELYK PFIIRKLIER GIVKTVKSAK KIVDRKEAVI
WDILEHVMKG HPVLLNRAPT LHRLGIQAFQ PKMIEGKAIQ LHPLACTAFN ADFDGDQMAV
HLPLSNEAIL EAQMLMLQSH NILNPANGAP ITVPAQDMVL GLYYITKLRA GAKGEGLTFY
GPEEALIAYN EGKVDIHAPV KVIVKDVDEN GNIVDVMRET SVGRVIVNEI VPPEAGYINT
IISKKSLRDI ISDVIKVCGV AKAADFLDGI KNLGYQMAFK GGLSFNLGDI IIPKEKETLV
QKGYDEVEQV VNNYNMGFIT NNERYNQVID IWTHVNSELS NILMKTISSD DQGFNSVYMM
LDSGARGSKE QIRQLSGMRG LMAKLQKAGA EGGQIIENPI LSNFKEGLSV LEYFISTHGA
RKGLADTALK TADAGYLTRR LVDVSHDVII TEEDCGTLRG LVCTDLKNND EVIATLYERI
LGRVSVHDII HPTTGELLVA GGEEITEEVA KKIQDSPIES VEIRSVLTCE AKKGVCAKCY
GRNLATSRMV QKGEAVGVIA AQSIGEPGTQ LTLRTFHAGG TAANIAANAS IVAKNSARLE
FEELRTVDIV DEMGEAAKVV VGRLAEVRFV DVNTGIVLST HNVPYGSTLY VSDGDLVEKG
KLIAKWDPFN AVIITEATGK IEFEGVIENV TYKVESDEAT GLREIIIIES KDKTKVPSAH
ILTEDGDLIR TYNLPVGGHV IIENGQKVKA GEVIVKIPRA VGKAGDITGG LPRVTELFEA
RNPSNPAVVS EIDGEVTMGK IKRGNREIIV TSKTGEVKKY LVALSKQILV QENDYVRAGT
PLSDGATTPA DILAIKGPTA VQEYIVNEVQ DVYRLQGVKI NDKHFEIIVR QMMRKVQIDE
PGDTRFLEQQ VVDKLEFMEE NDRIWGKKVV VDAGDSQNMQ PGQIVTARKL RDENSMLKRR
DLKPVEVRDA VAATSTQILQ GITRAALQTS SFMSAASFQE TTKVLNEAAI NGKTDKLEGM
KENVICGHLI PAGTGQREFE KIIVGSKEEY DRILANKKTV LDYNEVE
