RPOC_BIFLD
ID RPOC_BIFLD Reviewed; 1345 AA.
AC B3DTE1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=BLD_0964;
OS Bifidobacterium longum (strain DJO10A).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=205913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJO10A;
RX PubMed=18505588; DOI=10.1186/1471-2164-9-247;
RA Lee J.H., Karamychev V.N., Kozyavkin S.A., Mills D., Pavlov A.R.,
RA Pavlova N.V., Polouchine N.N., Richardson P.M., Shakhova V.V.,
RA Slesarev A.I., Weimer B., O'Sullivan D.J.;
RT "Comparative genomic analysis of the gut bacterium Bifidobacterium longum
RT reveals loci susceptible to deletion during pure culture growth.";
RL BMC Genomics 9:247-247(2008).
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; CP000605; ACD98410.1; -; Genomic_DNA.
DR RefSeq; WP_007051319.1; NZ_AABM02000002.1.
DR AlphaFoldDB; B3DTE1; -.
DR SMR; B3DTE1; -.
DR PRIDE; B3DTE1; -.
DR EnsemblBacteria; ACD98410; ACD98410; BLD_0964.
DR KEGG; blj:BLD_0964; -.
DR HOGENOM; CLU_000524_3_0_11; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000002419; 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..1345
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353299"
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 536
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 540
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 974
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 981
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 984
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1345 AA; 149265 MW; E755CDE20C110B3B CRC64;
MLDVNAFDKI RIGLATADDI RGWSHGEVKK PETINYRTLK PEKDGLFGEQ IFGPTRDWEC
ACGKYKRVRF KGIVCERCGV EVTRSRVRRE RMGHIELAAP VTHIWFFKGV PSRLGYLLNV
TPKDLERVIY FASYMVTEVN EDERHNDLPG LQDEFDSEIK RLEQRRDSDI EARAKKVEED
LAALEEAGEA KGPARTKLRN GAERDMAAIR TRYNDQIARV DAVFDKFKKL KPGDMVDDVD
LWREMQDRYG DYFDGCMGAE AIKKRLQSLD LETISKELRE EIKDASEQRK TKALKRLKVV
NAFLTTGNKP EAMVLDVIPV IPPDLRPMVQ LDGGRFATSD LNDLYRRVIN RNNRLKRLIE
LGAPEIMLNN EKRMLQEAVD SLFDNGRRGR PVTGASNRPL KSLSDMLKGK QGRFRQNLLG
KRVDYSGRSV IVVGPSLRMH QCGLPKPMAL ELFKPFVIKR LVDLNYAQNM KSAKRLVDRG
DAEVWGVLEE VISEHPVLLN RAPTLHRLGI QAFEPILVEG KAIHLPPLAC AAFNADFDGD
QMAVHLPLSA EAQAEARSLM MASDNILKPA DGHTVTMPSQ DMILGLYYLS TVLEGVKGQG
RVFSSLEEAE MALDRHEIDM QAKVLIRLPE SFVLPKNWEP GEVKVLDPRE GEDEVVKEER
FHDGTVLFAT SYGRILFNET LPTDYPFVNE QVAKGRLSKI VDDIAMRYST QQVAATLDAL
KDLGFTRAPW SGVSFAFSDV NEPPERDEKI AEYEAKADKV NANYEMGLLT EEARRQELID
LWTECTAEVS KEVEEKFDPT SNLAIIVQSG ARGNMMQINQ IAGMRGLVAN PKGEIIPRPV
KSNYRDGLSV LEYFISQHGA RKGLADTALR TAESGYLTRR LVDVSQDVIV REEDCGTKAG
LPIRVAERDN DGNLVLVKAA DGGPYSRLLA ADVIDPADGQ TVLYKRDDAL SMDVLNDLVA
HGVEEVKCRS VLTCESKRGV CAKCYGWSLA TNKLVDVGET VGIVAAQSIG EPGTQLTLRS
FHSGGVAAAS DITQGLPRVT ELFEARTPKG EAPITEFAGS IKIVENDRGR QIILTPDADS
GAPKEDGVIK PITYQVSKRV PLKVADGDHI KVGTQLVEGS VDPKKILTIL GKRAAQVNIV
EEVHTVYRSQ GVDIHDKHIE VIVHQMTRRV TIIDSGDTDL LPGELVDNAR FREINRNIVK
NGGRPAVGRP ALMGITKASL ATDSWLSAAS FQETTRVLTE AALSEKVDDL KGLKENVIIG
KLIPAGTGLA RYRNAVVEPD KAIRDTIYPN FGLGGDGDLG DASFSDADLS DLNFSNLEFG
DLKLGDDFNP DDFYSDQGGQ PDIEE
