ID RPOC_HYDS0 Reviewed; 1563 AA.
AC B4U738;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
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=HY04AAS1_0259;
OS Hydrogenobaculum sp. (strain Y04AAS1).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobaculum.
OX NCBI_TaxID=380749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y04AAS1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(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; CP001130; ACG56949.1; -; Genomic_DNA.
DR AlphaFoldDB; B4U738; -.
DR SMR; B4U738; -.
DR STRING; 380749.HY04AAS1_0259; -.
DR KEGG; hya:HY04AAS1_0259; -.
DR eggNOG; COG0086; Bacteria.
DR eggNOG; COG0433; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OrthoDB; 9815296at2; -.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR CDD; cd01609; RNAP_beta'_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 4.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 2.
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 NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1563
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353382"
FT BINDING 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 63
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 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 588
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
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 925
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 999
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1006
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"
SQ SEQUENCE 1563 AA; 176240 MW; 378A9AC000B028AB CRC64;
MKRGLLPFNK IKLLLASPEQ ILSWSHGEVK RPETLNYRTL KPEKEGLFCA KIFGPLKDYE
CLCGKYKGKR FEGTICDRCG VEVTKAYVRR ERFGHITLAT PCAHIWFLKS SPSKIGALLG
LSARDIEKVI YFESYLVVEY PTPDMEATFS NSENTIPVIK DGVTHHVKLH VVTEEQYEKE
FAYSIDNRYE SGMGAEFVRY VLSILDLETF AFKLKKILKP YTFGFEDLGP KMELEHKKLY
EKIIMFLADR VKLYSVGIAT SLNGVQMSIE DVIHGIVSES IYLNIKTGEI SNQDLGDDWY
TSKDAIRYRF EYVRGQNQNI PVFDKIQEDV RNIVLKDFSD TRVKNLVKTL KLVEGFLKSS
NRPEWMILTV LPVIPPELRP LVALDGGKFA TSDLNDLYRR LINRNNRLKR LIDLDAPDII
VRNEKRMLQE SVDVLIDNGK RGKVVSQHNR PLKSLSDYLK GKQGRFRQNL LGKRVDYSGR
SVIVVGPSLK MHQCGLPKIM ALELFKPFVY RRLEEKGYAT SIKNARKMVD QKQPEVWECL
EEVVKQHPVL LNRAPTLHRM SIQAFEPVLV EGKAIQLHPL VCPPFNADFD GDQMAVHVPL
GIEAQLESYI LILSTQNILS PANGRPIMLP SQDMVLGLFY ASNYVKGAKG EGKVFFSKED
AFLAFENKKI DIHAVIKVKI GDTFVETNIG RLLINEALPK GYRFVNEVLD KKSISKLIAD
IHKIYGSEIT AQTLDRLKEF GFEMATRAGI SIGIEDMKIP KAKKRLVDKA FHQMDEVLDQ
YRKGIITNKE RYNKTIDIWS QTTEDVTKAM FSEIEKSEQI ENGKKLPGLF NPIYMMANSG
ARGNKDQLRQ LAGMRGLMAK HSGEFIETPI TSNFREGLSV LEYFISTYGA RKGLADTALK
TSFAGYLTRR LVDVAQDMVI SEYDCGTKKY EVIEAIVESG EEKISLKERL IGRVLAEDIY
DPNSKELIAK ANDVLDEELT ARIQQAGVVQ VKARSVLNCE SENGICSMCY GWDLSQRKLV
SPGEAVGIIA AQSIGEPGTQ LTMRTFHIGG AATAQKVQSE LIIESSGIIK FQGLRLLKNR
NGGLINISQE GVIFVLDPNG RTIERHTVPY AAEILFKDGS EVKQGDIVAK WDPFNTYIIA
ESSGELVLKD IIVDVTVREE KDTLTGKTAI VVSFLRAKDA QLHSPRIVIK SEDGNEYSYD
LPVNSILNIP FEKLKTIWDK CLACSEAEKN DVQHNYYYLD KFVVHPGDII ARIPKETTKV
RDIVGGLPRV EELFEARKPK NPAIISEIDG IVKIYEDADE VMVISPKGTK KYDIKNEFIL
IKHGQEVKEG TKITDTIVSD VSGKAIVRAK GSKIVVYNKQ TGQEKVYSVP KGKFLQVKDG
DYVKVGDQLT DGTPLLEEIL KIKGIDELQK FLLKEVQMVY KLQGVDINDK HIEIIIRQML
RKRVIVDPGD SRFVANEEVD VIEFNKEVER IRKEDGKIPK AEPILVGITK AALSTKSWIS
AASFQETTRV LTEAASEGKV DDLSGIKENV IIGNLIPAGT GLEEYKNVKI EIAEHVTQFK
KQT
//
