RPOC_BIFAA
ID RPOC_BIFAA Reviewed; 1337 AA.
AC A1A316;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BAD_1318;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009256; BAF40099.1; -; Genomic_DNA.
DR RefSeq; WP_011743636.1; NC_008618.1.
DR AlphaFoldDB; A1A316; -.
DR SMR; A1A316; -.
DR STRING; 1680.BADO_1408; -.
DR PRIDE; A1A316; -.
DR EnsemblBacteria; BAF40099; BAF40099; BAD_1318.
DR KEGG; bad:BAD_1318; -.
DR HOGENOM; CLU_000524_3_0_11; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000008702; 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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1337
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308821"
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 1337 AA; 148153 MW; D782A1C466C23620 CRC64;
MLDVNEFDKL RIGLATADDI RNWSYGEVKK PETINYRTLK PEKDGLFGEQ IFGPTRDWEC
ACGKYKRVRF KGIVCERCGV EVTKSRVRRE RMGHIELAAP VTHIWFFKGV PSRLGYLLDI
APKDLEKVIY FAAYMVTKVD EEQRHQDLPD LQQEFDNEIA NLEKRRNAEI EERAKKVEAD
LAELEAEGEA KGSARAKLRN SAEREMAAIR TRYDEQIQRL SAVFDRFKTL KPGDMEGDVD
LWREMEDRYG DYFEGCMGAE AIKKRLQDFD LEAASKQLRE EIDTGTGQRK ARALKRLKVV
NAFLTTGNKP EAMVLDVIPV IPPDLRPMVQ LDGGRFATSD LNDLYRRVIN RNNRLKRLIE
LGAPEIMLNN EKRMLQEAVD SLFDNGRRGR PVTGASNRPL KSLSDMLKGK QGRFRQNLLG
KRVDYSGRSV IVVGPSLRMH QCGLPKPMAL ELFKPFVIKR LVDQGFAQNM KSAKRLVDRA
DSEVWGVLEE VISEHPVLLN RAPTLHRLGI QAFEPILVEG KAIHLPPLAC AAFNADFDGD
QMAVHLPLSA EAQAEARSLM MASDNILKPA DGHTVTMPSQ DMILGLYYLT TVIDGAKGQG
RVFSSLEEAE MALDKHEIDM QAKVLIRLPQ DFVLPKDWEP GEVKVVDPEP GSPDVVKEER
FHDGSVLFAT SYGRILFNGT LPVDYPFVNE QAPKKRLSKI VDDIATRYST AQVAATLDAL
KDLGFTRAPW SGVSFAFSDV IQPPELDEYI EKYEGEADKV NENYEIGMLT EEERRQELVD
LWTKCTSEVS EAVEEHFDSK NNLAIIVQSG ARGNMMQINQ IAGMRGLVAN PKGEIIPRPV
KSNYRKGLSV LEYFISQHGA RKGLADTALR TAESGYLTRR LVDVSQDVIV REEDCGTKRG
LTMKVGERDA EGNLHLVKAA DGGPYSRLLA ADVIDPADGE TVLYKAGDAL SMDVLNDLVA
HGVEEVKARS VLTCESKRGV CAKCYGWSLA TNKLVDVGEA VGIVAAQSIG EPGTQLTLRS
FHSGGVASAS DITQGLPRVT ELFEARTPKG EAPIAEFAGV VKVEDTERGR QVTLKPDDDS
VEPIVYPVTR RAPMLVKDGD HVEAGTQLIE GSVDPKKILR ILGPRAAQVN IVEEVHTVYR
SQGVDIHDKH IEVIVHQMLR RITVIDSGDT DLLPGELVDK ARFKAANMEA VKNGGKPAAG
RPELMGITKA SLATDSWLSA ASFQETTRVL TEAALNQKVD DLKGLKENVI IGKLIPAGTG
LARYRNATVE PDKAIRDTIY PNFGLGGEGT DSSFGDTDLS DVDFSNIDFG DLKLGDDFNP
DDFLDDNGGQ TDLGDTL
