RPOC_THET2
ID RPOC_THET2 Reviewed; 1524 AA.
AC Q72HM6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 106.
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=TT_C1460;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS81802.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE017221; AAS81802.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041443578.1; NC_005835.1.
DR AlphaFoldDB; Q72HM6; -.
DR SMR; Q72HM6; -.
DR STRING; 262724.TT_C1460; -.
DR PRIDE; Q72HM6; -.
DR EnsemblBacteria; AAS81802; AAS81802; TT_C1460.
DR KEGG; tth:TT_C1460; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000592; 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; 2.
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; 2.
DR SMART; SM00663; RPOLA_N; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1524
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067819"
FT REGION 1501..1524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 58
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 739
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 741
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 743
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1112
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1524 AA; 170718 MW; 9BBB7F593E2EB76B CRC64;
MKKEVRKVRI ALASPEKIRS WSYGEVEKPE TINYRTLKPE RDGLFDERIF GPIKDYECAC
GKYKRQRFEG KVCERCGVEV TKSIVRRYRM GHIELATPAA HIWFVKDVPS KIGTLLDLSA
TELEQVLYFS KYIVLDPKGA ILNGVPVEKR QLLTDEEYRE LRYGKQETYP LPPGVDALVK
DGEEVVKGQE LAPGVVSRLD GVALYRFPRR VRVEYVKKER AGLRLPLAAW VEKEAYKPGE
ILAELPEPYL FRAEEEGVVE LKELEEGAFL VLRQEDEPVA TYFLPVGMTP LVVHGEIVEK
GQPLAEAKGL LRMPRQVRAA QVEAEEEGET VYLTLFLEWT EPKDYRVQPH MNVVVPEGAR
VEAGDKIVAA IDPEEEVIAE AEGVVHLHEP ASILVVKARV YPFEDDVEVS TGDRVAPGDV
LADGGKVKSD VYGRVEVDLV RNVVRVVESY DIDARMGAEA IQQLLKELDL EALEKELLEE
MKHPSRARRA KARKRLEVVR AFLDSGNRPE WMILEAVPVL PPDLRPMVQV DGGRFATSDL
NDLYRRLINR NNRLKKLLAQ GAPEIIIRNE KRMLQEAVDA LLDNGRRGAP VTNPGSDRPL
RSLTDILSGK QGRFRQNLLG KRVDYSGRSV IVVGPQLKLH QCGLPKRMAL ELFKPFLLKK
MEEKGIAPNV KAARRMLERQ RDIKDEVWDA LEEVIHGKVV LLNRAPTLHR LGIQAFQPVL
VEGQSIQLHP LVCEAFNADF DGDQMAVHVP LSSFAQAEAR IQMLSAHNLL SPASGEPLAK
PSRDIILGLY YITQVRKEKK GAGLEFATPE EALAAHERGE VALNAPIKVA GRETSVGRLK
YVFANPDEAL LAVAHGIVDL QDVVTVRYMG KRLETSPGRI LFARIVAEAV EDEKVAWELI
QLDVPQEKNS LKDLVYQAFL RLGMEKTARL LDALKYYGFT FSTTSGITIG IDDAVIPEEK
KQYLEEADRK LLQIEQAYEM GFLTDRERYD QILQLWTETT EKVTQAVFKN FEENYPFNPL
YVMAQSGARG NPQQIRQLCG MRGLMQKPSG ETFEVPVRSS FREGLTVLEY FISSHGARKG
GADTALRTAD SGYLTRKLVD VTHEIVVREA DCGTTNYISV PLFQPDEVTR SLRLRKRADI
EAGLYGRVLA REVEVLGVRL EEGRYLSMDD VHLLIKAAEA GEIQEVPVRS PLTCQTRYGV
CQKCYGYDLS MARPVSIGEA VGIVAAQSIG EPGTQLTMRT FHTGGVAGAA DITQGLPRVI
ELFEARRPKA KAVISEIDGV VRIEETEEKL SVFVESEGFS KEYKLPKEAR LLAKDGDYVE
AGQPLTRGAI DPHQLLEAKG PEAVERYLVE EIQKVYRAQG VKLHDKHIEI VVRQMMKYVE
VTDPGDSRLL EGQVLEKWDV EALNERLIAE GKTPVAWKPL LMGVTKSALS TKSWLSAASF
QNTTHVLTEA AIAGKKDELI GLKENVILGR LIPAGTGSDF VRFTQVVDQK TLKAIEEARK
EAVEAKERPA ARRGVKREQP GKQA
