RPOC_AROAE
ID RPOC_AROAE Reviewed; 1409 AA.
AC Q5P338;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, 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=AZOSEA21510;
GN ORFNames=ebA3819;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI08276.1; -; Genomic_DNA.
DR RefSeq; WP_011237967.1; NC_006513.1.
DR AlphaFoldDB; Q5P338; -.
DR SMR; Q5P338; -.
DR STRING; 76114.ebA3819; -.
DR EnsemblBacteria; CAI08276; CAI08276; ebA3819.
DR KEGG; eba:ebA3819; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000006552; 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; -; 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..1409
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225506"
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 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 466
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 1409 AA; 155260 MW; A77E0C927A4A879E CRC64;
MKSLLADLFK QTLPNEDQFD AITIGLASPD KIRSWSYGEV KKPETINYRT FKPERDGLFC
AKIFGPVKDY ECLCGKYKRL KHRGVICEKC GVEVTLSKVR RERMAHIELA SPTAHIWFLK
SLPSRLGMVL DMTLRDIERV LYFEAFVVVE PGMTPLNRGQ LLTEDDYLAK VEEYGDDFDA
LMGAEGIRGL LRTLDVKLEI EKLRGDLETT GSEAKIKKFS KRLKVLEAFM QSGIKPEWMI
LEVLPVLPPD LRPLVPLDGG RFATSDLNDL YRRVINRNNR LKRLLELKAP EIIVRNEKRM
LQESVDSLLD NGRRGKAMTG ANKRPLKSLA DMIKGKGGRF RQNLLGKRVD YSGRSVIVVG
PQLKLHQCGL PKLMALELFK PFIFNKLELM GLATTIKQAK KMVESQEPVV WDILEEVIRE
HPVMLNRAPT LHRLGIQAFE PVLIEGKAIQ LHPLVCVAFN ADFDGDQMAV HVPLSLEAQM
EARTLMLASN NVLSPANGEP IIVPSQDIVL GLYYATREGV NVAGEGMAFS DVGELKRAYE
SKQLSLHARV SVRLKEVEVS AEGERRDKIT RYNTTAGRAM LSEILPPGLP FSVLDKALKK
KEISRLINAS FRRCGLKETV VFADKLMQFG FRLATRAGIS IAVKDMLVPR QKDVLIHAAE
QEVKEIARQY TSGLVTDGER YNKVVDIWGR AGDQVAKAMM DQLGQEDVVN RHGDTVKQES
FNSIYMMADS GARGSAAQIR QLAGMRGLMA KPDGSIIETP ITTNFREGLN VLQYFISTHG
ARKGLADTAL KTANSGYLTR RLVDVTQDLV VTEDDCGTRD GFVMKALIEG GEVIEPLRDR
ILGRVCAEDV VNPESQETVI EAGSLLGEDA VDLIESLGID EVKVRTALTC ETRYGLCGKC
YGRDLGRGSQ VNVGEAVGVI AAQSIGEPGT QLTMRTFHVG GAASRAAAAS GVESKSAGTV
RFAGNMRYVS NAKGEKIIIA RSAEVVVADD MGRERERHKL PYGATLLVDD GAPVKAGVLL
ATWDPHTRPI VTEYSGTVKF ENVEEGATVA KQIDEVTGLS TLVVIDGKRR TSGASSKGVR
PQVKLLDERG EEVKIAGTDH SVAITFQVGS LITVKDGQEV SVGDILARIP QESAKTRDIT
GGLPRVAELF EARPPKDAGV LAEYTGTVSF GKDTKGKQRL VITEADGTAH EFLIPKDKHV
MVHDGQVVNK GELIVDGPAD PHDILRLQGI EALARYIIDE VQDVYRLQGV KINDKHIEVI
VRQMLRRVVI NDAGNSRFIR EEQVERSEVL DENDRIEAEG KLPAQYQNVL LGITKASLST
DSFISAASFQ ETTRVLTEAA IMGKRDDLRG LKENVIVGRL IPAGTGMAYH RNRKAQNAGE
DLGPEHAWAE MQEVVPEVPA DVSQDVQAG
