RPOC_GRABC
ID RPOC_GRABC Reviewed; 1387 AA.
AC Q0BUQ5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=GbCGDNIH1_0549;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI61447.1; -; Genomic_DNA.
DR RefSeq; WP_011631257.1; NC_008343.2.
DR AlphaFoldDB; Q0BUQ5; -.
DR SMR; Q0BUQ5; -.
DR STRING; 391165.GbCGDNIH1_0549; -.
DR PRIDE; Q0BUQ5; -.
DR EnsemblBacteria; ABI61447; ABI61447; GbCGDNIH1_0549.
DR KEGG; gbe:GbCGDNIH1_0549; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000001963; 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; -; 2.
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..1387
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353376"
FT REGION 1367..1387
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 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 463
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 465
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 808
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 882
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 892
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1387 AA; 154355 MW; D8E8327D332852D8 CRC64;
MNELMKILGQ GGQSLSFDQI KIQMASPEQI RSWSYGEIKK PETINYRTFK PERDGLFCAR
IFGPIKDYEC LCGKYKRMKF RGIVCEKCGV EVTLAKVRRE RMGHIELASP VAHIWFLKSL
PSRIGLMVDL TLKELEKILY FENYVVLEPG LTDLKLHQLL TEEQLLNKQD EFGDDAFRAG
IGAEAIKSVL EGIDIDEDKV RLRAELKETT SETKRKKLVK RLKLIEAFAE SGAKPEWMIL
DVVPVIPPEL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLIELRAPD IIVRNEKRML
QESVDALFDN GRRGRAITGA NKRPLKSLSD MLKGKQGRFR QNLLGKRVDY SGRSVIVVGP
EMKLHQCGLP KKMALELFKP FIYSKLEKYG HATTIKAAKR MVEKERPEVW DILEEVIREH
PVMLNRAPTL HRLGIQAFEP VLIEGKAIQL HPLVTTAFNA DFDGDQMAVH VPLSLEAQLE
ARVLMMSTNN ILSPANGKPI IVPSQDIVLG LYYLSLETPE FRNTPDDKAQ AFGTLGEIEA
ALHARTVTLH TKIRARLHTV DDQGSPIRVR VVTTPGRMLI AQILPRHPNV PFALINKQLT
KKNVSDVIDA VYRHCGQKEC VIFADRLMGL GFGQAAKAGI SFGKDDLIIP AEKQEMIEKT
AGEVKEFEQQ YQDGLITAGE RYNKVVDAWS RCTDEVAGAM MKEISKQELG RPINSVWMMS
HSGARGSPAQ MRQLAGMRGL MAKPSGEIIE QPIIANFKEG LSVLEYFNST HGARKGLADT
ALKTANSGYL TRRLVDVAQD CIIVENDCGT ERGLTVRAVM DGGEVVSSLS ERILGRTLSE
DVLDPTTNKI LYPRNTLIEE EHAEKIEKAG IEVVKIRSVL TCESTVGVCG HCYGRDLARG
TPVNIGEAVG VIAAQSIGEP GTQLTMRTFH IGGAAQRGAE QSSVEASHDG IVTVKNRNVV
LNSQNVAIVM SRNCEIVLAD EKGRERARYR VPYGARLLTD EGAQVTRAQK LAEWDPYTLP
IITERAGKVE YLDLLDGVTL VERMDEVTGL TSKVVVDYKQ NARGVDLRPR LQLKDESGDV
VRLSNNTDAR YFLSPDSILS VENGAEVNAG DVLARIPREG SKTRDITGGL PRVAELFEAR
RPKDHAVIAE TDGRVEFGKD YKAKRRIIVK NDETGEETEY LIPKGKHVSV QEGDFVRLGD
PLVDGPRVPH DILKVLGVEA LSDYLVNEIQ DVYRLQGVKI NDKHIEVIVR QMLQKVEILD
PGDTMYLIGE QVDRLEFEAE NRKREREGER PAVAMPVLQG ITKASLQTQS FISAASFQET
TRVLTEAATA GKVDTLNGLK ENVIVGRLIP AGTGSVMNRL RRIASGQDEA KGVGQETPRL
SGQEAAE
