RPOC_AQUAE
ID RPOC_AQUAE Reviewed; 1574 AA.
AC O67763;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=aq_1945;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC07724.1; -; Genomic_DNA.
DR PIR; G70466; G70466.
DR RefSeq; NP_214332.1; NC_000918.1.
DR RefSeq; WP_010881268.1; NC_000918.1.
DR AlphaFoldDB; O67763; -.
DR SMR; O67763; -.
DR STRING; 224324.aq_1945; -.
DR PRIDE; O67763; -.
DR EnsemblBacteria; AAC07724; AAC07724; aq_1945.
DR KEGG; aae:aq_1945; -.
DR PATRIC; fig|224324.8.peg.1502; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR InParanoid; O67763; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000798; 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 InterPro; IPR011054; Rudment_hybrid_motif.
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 SUPFAM; SSF51246; SSF51246; 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..1574
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067701"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 590
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 592
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 594
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1002
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1009
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1012
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1574 AA; 178501 MW; 4E61AF291FEF7E78 CRC64;
MSEARRGIFP FSKIKLMLAS PEDIRSWSHG EVKRPETLNY RTLKPEKDGL FCAKIFGPIK
DYECLCGKYR GKRYEGKICE KCGVEVTTSY VRRQRFGHIE LAAPVVHIWF LKSTPSKIGT
LLNLTSRDVE RVAYFESYLV IEYPNEEEEE KFEKDEHTIP LNDGISTKWV KLHVVNEEEF
EEKYAFTIDE KYEHGMGAEI LKEVLSKLDL DAYSRKLKEI VKPYSIGFED LGKEIEQKYK
NLYQKLIKVI ADDFRAYGVE IKGLEDHGLS LEQAIHRILN EELYLNVETG EISLEDCGDS
CLTGRDALKE YYERVREHKK DIPIFEKIKE DIRSTVLREI SEARIRKALR TLQLVEGFKK
SGNRPEWMIL EVLPVLPPEL RPLVALDGGR FATSDLNDFY RRVINRNNRL KRLIELNAPD
IIIRNEKRML QEAVDALIDN GKRGNPVKQN GRPLKSLADY LKGKQGRFRQ NLLGKRVDYS
GRSVIVVGPE LQMHQCGLPK IMALELFKPF VYRRLEEKGY ATSIKHAKRL VEQKTPEVWE
CLEEVVKEHP VLLNRAPTLH RPSIQAFEPV LVEGKAIQLH PLVCPPFNAD FDGDQMAVHV
PLGIEAQLES YILMLSTQNV LSPAHGKPLT MPSQDMVLGT YYITHDPIPG RKGEGKAFGT
FEEVLKALEL GHVDIHAKIK VKVGNEWIET TPGRVLFNSI MPEGQPFVNK TLDKKGLSKL
ITELYIRVGN EETVKFLDRV KELGFLRSTL AGISIGVEDL QVPKAKKKII EEALKKTEEI
WNQYVQGIIT NKERYNRIID VWSEATNLVS KAMFEEIEKS KRIENGKEYP GTFNPIYMMA
ISGARGNRDQ IRQLAGMRGL MAKHSGEFIE TPIISNFREG LSVLEYFIST YGARKGLADT
ALKTAFAGYL TRRLVDVAQD ITITERDCGT VKGFEMEPIV EAGEERVPLK DRIFGRVLAE
DVKDPYTGEI IARRNEVIDE KLAEKITKAG IEKVRVRSPL TCEAKHGVCA MCYGWDLSQR
KIVSVGEAVG IIAAQSIGEP GTQLTMRTFH IGGAATAQKV QSFVKAESDG KVKFYNVKLI
VNRKGEKINI SKDAAIGIVD EEGRLLERHT IPYGARILVE EGQEVKAETK LADWDPFNTY
IIAEVGGKVE LRDIILDVTV REERDPITGK TASVISFMRP RDAMLHTPRI AVITEDGKEY
IYDLPVNAIL NIPPEKISLE WRVCPTCSES EETTIQHQYY VVKDLEVQPG DILARIPKET
AKVRDIVGGL PRVEELFEAR KPKNPAILSE IDGYVKIYED ADEVIIFNPR TGETAKYSIK
KDELILVRHG QFVKKGQKIT ETKVAEIDGQ VRIKGRGFKV IVYNPETGLQ REYFVPKGKF
LLVKEGDFVK AGDQLTDGTP VPEEILRIKG IEELEKFLLK EVQMVYKLQG VDINDKHFEI
IIKQMLKKVR IIDPGDSRFL VGEEVDKEEL EEEIQRIKLE GGKLPKAEPV LVGITRAALS
TRSWISAASF QETTRVLTDA SVEGKIDELR GLKENVIIGN IIPAGTGVDE YREVDVIPAE
EKVLEEKKEP KEGS
