RPOC_DECAR
ID RPOC_DECAR Reviewed; 1403 AA.
AC Q47JA9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Daro_0313;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(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; CP000089; AAZ45072.1; -; Genomic_DNA.
DR RefSeq; WP_011286082.1; NC_007298.1.
DR AlphaFoldDB; Q47JA9; -.
DR SMR; Q47JA9; -.
DR STRING; 159087.Daro_0313; -.
DR PRIDE; Q47JA9; -.
DR EnsemblBacteria; AAZ45072; AAZ45072; Daro_0313.
DR KEGG; dar:Daro_0313; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
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..1403
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225528"
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 816
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 890
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 897
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"
SQ SEQUENCE 1403 AA; 155039 MW; 5C180D686FC73C3F CRC64;
MKALLDLFKQ VTAEEEFDAI TIGLASPDKI RSWSYGEVKK PETINYRTFK PERDGLFCAK
IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTLAKVRRD RMGHIELASP TAHIWFLKSL
PSRLGMVLDM TLRDIERVLY FEAYVVTDPG MVSNLQRAQL LTEDQYLEMV EEHGDEFQAL
MGAEGIRELL RNLELDSEVE SLHAELEVTG SEAKNKKLAK RLKILEGFQK SGIKPDWMIL
EVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLELKAPE IIVRNEKRML
QESVDSLLDN GRRGKAMTGA NKRPLKSLAD MIKGKGGRFR QNLLGKRVDY SGRSVIVVGP
QLKLHQCGLP KLMALELFKP FIFHKLEVLG YATTIKQAKK MVEGQEPVVW DILEDVIREH
PVMLNRAPTL HRLGIQAFEP TLIEGKAIQL HPLVCAAFNA DFDGDQMAVH VPLSLEAQME
ARTLMLASNN VLSPANGQPI IVPSQDIVLG LYYATREKIN GKGEGMYFAD TAEIERAMAA
GQLDVHSRIS VRLKQYEPAA VDGEWEEKTV RVETTAGRAL LAKILPKGLP FKAIDRALKK
KEISKLIDES FRRCGLKETV IFADKLMQNG YALATRAGIS FCSDDMLVPA KKYEIISSAE
AEVKEIETQY TNGLVTQGER YNKVVDIWGR TGDQVAKVMM EELGHEEVID RHGKKVKQDS
FNSIYMMADS GARGSAAQIR QLAGMRGLMA KPDGSIIETP ITTNFREGLN VLQYFISTHG
ARKGLADTAL KTANSGYLTR RLVDVTQDLV ITEDDCGTKN GFVVKALVEG GEVIEALRER
ILGRVTVDDL IDPETQETVI FAGTMLDEDL VDLIDKLGID EVKVRTPLTC DTRYGLCAQC
YGRDLGRGTM VNAGEAVGVI AAQSIGEPGT QLTMRTFHVG GAASRAAVAD KVEGKSAGTV
RYTSNMRYVT SAKGEKVVIS RSGEVLIVDD HGRERERHKV PYGAMLSVDE DKSVKAGAKL
ATWDPHTRPI ITEYAGTVRF ENVEEGVTVA KQVDDVTGLS TLVVIDHKRG GKAAVKGVRP
VVKLLDESGQ EVRVHGSDHT VSIAFQVGSI ISVVDGQQVG VGDVLARMPQ ESAKTRDITG
GLPRVAELFE ARTPKDASVL AEVTGTISFG KDTKGKQRLV ITDLEGNVHE FLISKDKHVL
VHDGQVVNKG EKIVEGEPDP HDILRLQGIE ALARYITDEV QDVYRLQGVK INDKHIEVIV
RQMLRRVTIV EPGDTKFIKS EQVERAELLA ENDRANAEGK IPATIEHMLL GITKASLSTD
SFISAASFQE TTRVLTEAAI MGKRDELRGL KENVIVGRLI PAGTGLAFHR SRKAQLAGED
IAASRQIEEA TAENTTQEAD QGL
