RPOC_MYCBT
ID RPOC_MYCBT Reviewed; 1316 AA.
AC C1AL01;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 69.
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=JTY_0687;
OS Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=561275;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BCG / Tokyo 172 / ATCC 35737 / TMC 1019;
RX PubMed=19200449; DOI=10.1016/j.vaccine.2009.01.034;
RA Seki M., Honda I., Fujita I., Yano I., Yamamoto S., Koyama A.;
RT "Whole genome sequence analysis of Mycobacterium bovis bacillus Calmette-
RT Guerin (BCG) Tokyo 172: a comparative study of BCG vaccine substrains.";
RL Vaccine 27:1710-1716(2009).
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; AP010918; BAH24980.1; -; Genomic_DNA.
DR RefSeq; WP_012666331.1; NZ_CP014566.1.
DR AlphaFoldDB; C1AL01; -.
DR SMR; C1AL01; -.
DR KEGG; mbt:JTY_0687; -.
DR HOGENOM; CLU_000524_3_1_11; -.
DR OMA; YRNIRVE; -.
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; 1.
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..1316
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000165845"
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 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 968
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 975
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 978
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1316 AA; 146682 MW; 3E7B508FDB5F5297 CRC64;
MLDVNFFDEL RIGLATAEDI RQWSYGEVKK PETINYRTLK PEKDGLFCEK IFGPTRDWEC
YCGKYKRAPF KGIICERCGV EVTRAKVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDL
APKDLEKIIY FAAYVITSVD EEMRHNELST LEAEMAVERK AVEDQRDGEL EARAQKLEAD
LAELEAEGAK ADARRKVRDG GEREMRQIRD RAQRELDRLE DIWSTFTKLA PKQLIVDENL
YRELVDRYGE YFTGAMGAES IQKLIENFDI DAEAESLRDV IRNGKGQKKL RALKRLKVVA
AFQQSGNSPM GMVLDAVPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLKRLIDL
GAPEIIVNNE KRMLQESVDA LFDNGRRGRP VTGPGNRPLK SLSDLLKGKQ GRFRQNLLGK
RVDYSGRSVI VVGPQLKLHQ CGLPKLMALE LFKPFVMKRL VDLNHAQNIK SAKRMVERQR
PQVWDVLEEV IAEHPVLLNR APTLHRLGIQ AFEPMLVEGK AIQLHPLVCE AFNADFDGDQ
MAVHLPLSAE AQAEARILML SSNNILSPAS GRPLAMPRLD MVTGLYYLTT EVPGDTGEYQ
PASGDHPETG VYSSPAEAIM AADRGVLSVR AKIKVRLTQL RPPVEIEAEL FGHSGWQPGD
AWMAETTLGR VMFNELLPLG YPFVNKQMHK KVQAAIINDL AERYPMIVVA QTVDKLKDAG
FYWATRSGVT VSMADVLVPP RKKEILDHYE ERADKVEKQF QRGALNHDER NEALVEIWKE
ATDEVGQALR EHYPDDNPII TIVDSGATGN FTQTRTLAGM KGLVTNPKGE FIPRPVKSSF
REGLTVLEYF INTHGARKGL ADTALRTADS GYLTRRLVDV SQDVIVREHD CQTERGIVVE
LAERAPDGTL IRDPYIETSA YARTLGTDAV DEAGNVIVER GQDLGDPEID ALLAAGITQV
KVRSVLTCAT STGVCATCYG RSMATGKLVD IGEAVGIVAA QSIGEPGTQL TMRTFHQGGV
GEDITGGLPR VQELFEARVP RGKAPIADVT GRVRLEDGER FYKITIVPDD GGEEVVYDKI
SKRQRLRVFK HEDGSERVLS DGDHVEVGQQ LMEGSADPHE VLRVQGPREV QIHLVREVQE
VYRAQGVSIH DKHIEVIVRQ MLRRVTIIDS GSTEFLPGSL IDRAEFEAEN RRVVAEGGEP
AAGRPVLMGI TKASLATDSW LSAASFQETT RVLTDAAINC RSDKLNGLKE NVIIGKLIPA
GTGINRYRNI AVQPTEEARA AAYTIPSYED QYYSPDFGAA TGAAVPLDDY GYSDYR
