RPOC_BACFR
ID RPOC_BACFR Reviewed; 1427 AA.
AC Q64NJ8;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=BF4191;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP006841; BAD50934.1; -; Genomic_DNA.
DR RefSeq; WP_005804126.1; NZ_UYXF01000007.1.
DR RefSeq; YP_101468.1; NC_006347.1.
DR AlphaFoldDB; Q64NJ8; -.
DR SMR; Q64NJ8; -.
DR STRING; 295405.BF4191; -.
DR PRIDE; Q64NJ8; -.
DR EnsemblBacteria; BAD50934; BAD50934; BF4191.
DR KEGG; bfr:BF4191; -.
DR PATRIC; fig|295405.11.peg.4046; -.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002197; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1427
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067705"
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; 158598 MW; 7A5A50C7C677F011 CRC64;
MAFRKENKIK SNFSKISIGL ASPEEILENS SGEVLKPETI NYRTYKPERD GLFCERIFGP
IKDYECHCGK YKRIRYKGIV CDRCGVEVTE KKVRRERMGH IQLVVPVAHI WYFRSLPNKI
GYLLGLPTKK LDSIIYYERY VVIQPGVKAE DGIAEFDLLS EEEYLDILDT LPKDNQYLED
TDPNKFIAKM GAEAIYDLLA RLDLDALSYE LRHRAGNDAS QQRKNEALKR LQVVESFRAS
RGRNKPEWMI VRIVPVIPPE LRPLVPLDGG RFATSDLNDL YRRVIIRNNR LKRLIEIKAP
EVILRNEKRM LQESVDSLFD NSRKSSAVKT DANRPLKSLS DSLKGKQGRF RQNLLGKRVD
YSARSVIVVG PELRMHECGI PKLMAAELYK PFIIRKLIER GIVKTVKSAK KIVDRKEPVI
WDILEHVMKG HPVLLNRAPT LHRLGIQAFQ PKMIEGKAIQ LHPLACTAFN ADFDGDQMAV
HLPLSNEAVL EAQMLMLASH NILNPANGAP ITVPSQDMVL GLYYITKLRK GAKGEGLTFY
GPEEALIAYN EGKVDIHAPV KVIVKDLDEN GNIVDVMRET SVGRVIVNEI VPPEVGYINT
IISKKSLRDI ISAVIKACGV ARTADFLDGI KNLGYKMAFQ GGLSFNLGDI IIPKEKETLV
QRGYEEVEQV ISNYNMGFIT NNERYNQVID IWTHVNSELS NILMKTISSD DQGFNSVYMM
LDSGARGSKE QIRQLSGMRG LMAKPQKAGA EGGQIIENPI LSNFKEGLSV LEYFISTHGA
RKGLADTALK TADAGYLTRR LVDVSHDVII NEEDCGTLRG LVCTDLKNND EVIATLYERI
LGRVSVHDII HPQTGELLVA GGEEITEDIA KKIQESPIES VEIRSVLTCE SKKGVCAKCY
GRNLATNHMV QKGEAVGVIA AQSIGEPGTQ LTLRTFHAGG TAANIAANAS IVAKNNARLE
FEELRTVDIV DETGEAAKVV VGRLAEVRFI DVNTGIVLST HNVPYGSTLY VADGEVVEKG
KLIAKWDPFN AVIITEATGK IEFEGVIENV TYKIESDEAT GLREIIIIES KDKTKVPSAH
ILTEDGDLIR TYNLPVGGHV VIENGQKVKA GEVIVKIPRA VGKAGDITGG LPRVTELFEA
RNPSNPAVVS EIDGEVTMGK VKRGNREIIV TSKTGEVKKY LVPLSKQILV QENDYVRAGT
PLSDGATTPA DILAIKGPTA VQEYIVNEVQ DVYRLQGVKI NDKHFEIIVR QMMRKVTIDE
PGDTRFLEQQ VVDKLEFMEE NDRIWGKKVV VDAGDSENLK AGQIVTARKL RDENSMLKRR
DLKPVEVRDA VAATSTQILQ GITRAALQTS SFMSAASFQE TTKVLNEAAI NGKIDKLEGM
KENVICGHLI PAGTGLREFD KIIVGSKEEY DRILANKKTV LDYNEVE
