ID   RPOC_BURMA              Reviewed;        1412 AA.
AC   Q62GJ7;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=BMA2640;
OS   Burkholderia mallei (strain ATCC 23344).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=243160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23344;
RX   PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA   Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA   Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA   Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA   Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA   Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA   Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT   "Structural flexibility in the Burkholderia mallei genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(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}.
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DR   EMBL; CP000010; AAU47878.1; -; Genomic_DNA.
DR   RefSeq; WP_004198364.1; NC_006348.1.
DR   RefSeq; YP_104174.1; NC_006348.1.
DR   AlphaFoldDB; Q62GJ7; -.
DR   SMR; Q62GJ7; -.
DR   STRING; 243160.BMA2640; -.
DR   EnsemblBacteria; AAU47878; AAU47878; BMA2640.
DR   GeneID; 56594535; -.
DR   KEGG; bma:BMA2640; -.
DR   PATRIC; fig|243160.12.peg.2713; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_4; -.
DR   OMA; YRNIRVE; -.
DR   Proteomes; UP000006693; Chromosome 1.
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..1412
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000225517"
FT   REGION          1393..1412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         819
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         893
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         900
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         903
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1412 AA;  155934 MW;  AF57A2C68C937C99 CRC64;
     MKALLDLFKQ VQQEEIFDAI KIGLASPDKI RSWSFGEVKK PETINYRTFK PERDGLFCAK
     IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTLAKVRRE RMGHIELASP VAHIWFLKSL
     PSRLGMVLDM TLRDIERVLY FEAYVVIDPG MTPLKARQIM TEEDYYNKVE EYGDEFRAEM
     GAEGVRELLR SINIDEQVET LRTELKNTGS EAKIKKYAKR LKVLEAFQRS GIKPDWMILE
     VLPVLPPELR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLELKAPEI IVRNEKRMLQ
     EAVDSLLDNG RRGKAMTGAN KRPLKSLADM IKGKGGRFRQ NLLGKRVDYS GRSVIVVGPT
     LKLHQCGLPK LMALELFKPF IFNKLEVMGV ATTIKAAKKE VENQTPVVWD ILEEVIREHP
     VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAFNAD FDGDQMAVHV PLSLEAQMEA
     RTLMLASNNV LFPANGDPSI VPSQDIVLGL YYATREAING KGEGLSFTGV SEVIRAYENK
     EVELASRVNV RITEMVRNED TSEGAPQFVP KISLYATTVG RAILSEILPP GLPFSVLNKP
     LKKKEISRLI NTAFRKCGLR ATVVFADQLM QSGFRLATRA GISICVDDML VPTQKETIVG
     DAAKKVKEYD RQYMSGLVTA QERYNNVVDI WSATSEAVGK AMMEQLSTEP VIDRGGNETR
     QESFNSIYMM ADSGARGSAV QIRQLAGMRG LMAKPDGSII ETPITANFRE GLNVLQYFIS
     THGARKGLAD TALKTANSGY LTRRLVDVTQ DLVVVEDDCG TSNGVAMKAL VEGGEVVEAL
     RDRILGRVAA SDVVNPETQE TLYEAGALLD ETAVEDIERL GIDEVRVRTA LTCETRYGLC
     ASCYGRDLGR GSLVNVGEAV GVIAAQSIGE PGTQLTMRTF HIGGAASRAA VASSVEAKSN
     GTVRFTASMR YVTNAKGEQI VISRSGEALI TDDIGRERER HKIPYGATLL QLDGAAIKAG
     TQLATWDPLT RPIITEYGGT VKFENVEEGV TVAKQIDDVT GLSTLVVIDV KRRGSQAAKS
     VRPQVKLLDA NGDEVKIPGT EHAVQIGFQV GALITVKDGQ QVQVGEVLAR IPTESQKTRD
     ITGGLPRVAE LFEARSPKDA GILAEVTGTV SFGKDTKGKQ RLVITDLEGN QHEFLIAKEK
     QVLVHDGQVV NKGEMIVDGP ADPHDILRLQ GIEALSRYIV DEVQDVYRLQ GVKINDKHIE
     VIVRQMLRRV QIVDNGDTRF IPGEQVERSD MLDENDRMIA EDKRPATYDN ILLGITKASL
     STDSFISAAS FQETTRVLTE AAIMGKRDDL RGLKENVIVG RLIPAGTGLA FHKARKAKEQ
     SDRERFDQIA AEEAFEFGTP SAPAEEPQHP AE