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RPOC_BURM1
ID   RPOC_BURM1              Reviewed;        1413 AA.
AC   A9ADI6;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, 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};
GN   OrderedLocusNames=Bmul_0242, BMULJ_03012;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) 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; CP000868; ABX13937.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44897.1; -; Genomic_DNA.
DR   RefSeq; WP_006400664.1; NC_010804.1.
DR   AlphaFoldDB; A9ADI6; -.
DR   SMR; A9ADI6; -.
DR   STRING; 395019.Bmul_0242; -.
DR   PRIDE; A9ADI6; -.
DR   EnsemblBacteria; BAG44897; BAG44897; BMULJ_03012.
DR   GeneID; 66525169; -.
DR   KEGG; bmj:BMULJ_03012; -.
DR   KEGG; bmu:Bmul_0242; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_4; -.
DR   OMA; YRNIRVE; -.
DR   Proteomes; UP000008815; 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; Reference proteome; Transcription; Transferase;
KW   Zinc.
FT   CHAIN           1..1413
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353312"
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   1413 AA;  156178 MW;  F415991B5883D84D CRC64;
     MKALLDLFKQ VQQEEVFDAI KIGLASPDKI RSWSFGEVKK PETINYRTFK PERDGLFCAK
     IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTLAKVRRE RMGHIELASP VAHIWFLKSL
     PSRLGMVLDM TLRDIERVLY FEAYVVIDPG MTPLKARQIM TEEDYYNKVE EYGDEFRAEM
     GAEGVRELLR AINIDEQVEQ LRTELKNTGS EAKIKKYAKR LKVLEAFQRS GIKPEWMILE
     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 KGEGLTFTGV SEVIRAYENK
     EVELASRVNV RITEMVRNED KSEGAPEFVP KISLYATTVG RAILSEILPP GLPFSVLNKP
     LKKKEISRLI NTAFRKCGLR ATVVFADQLM QSGFRLATRA GISICVDDML VPPQKETIVG
     DAAKKVKEYD RQYMSGLVTA QERYNNVVDI WSATSEAVGK AMMEQLSTEP VIDRDGNETR
     QESFNSIYMM ADSGARGSAV QIRQLAGMRG LMAKPDGSII ETPITANFRE GLNVLQYFIS
     THGARKGLAD TALKTANSGY LTRRLVDVTQ DLVVVEDDCG TSNGVAMKAL VEGGEVVEAL
     RDRILGRVAV ADVVNPETQE TLYEAGTLLD ETAVEEIERL GIDEVRVRTP LTCETRYGLC
     ASCYGRDLGR GTLVNVGEAV GVIAAQSIGE PGTQLTMRTF HIGGAASRAA VASSVEAKSN
     GTVRFSPSMR YVTNAKGEQI VISRSGEALI TDDIGRERER HKIPYGATLL QLDGAAIKAG
     TQLATWDPMT RPIITEYGGT VKFENVEEGV TVAKQIDDVT GLSTLVVIDA KRRGSQASKS
     VRPQVKLLDA NGDEVKIPGT EHSVQIGFQV GALITVKDGQ QVQVGEVLAR IPTESQKTRD
     ITGGLPRVAE LFEARSPKDA GILAEVTGTV SFGKDTKGKQ RLVITDLEGN QHEFLIAKEK
     QVLVHDGQVV NKGEMIVDGP ADPHDILRLQ GIEALSRYIV DEVQDVYRLQ GVKINDKHIE
     VIVRQMLRRV QITDNGDSRF IPGEQVERSD MLDENDRMIA EGKRPASYEN VLLGITKASL
     STDSFISAAS FQETTRVLTE AAIMGKRDDL RGLKENVIVG RLIPAGTGLA FHKARKAKEM
     SDRERFDQIA AEEAFDFGTP STPAEEPQHP AAE
 
 
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