RPOC_SULSY
ID RPOC_SULSY Reviewed; 1579 AA.
AC B2V7L9;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, 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=SYO3AOP1_0297;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
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; CP001080; ACD65942.1; -; Genomic_DNA.
DR RefSeq; WP_012459030.1; NC_010730.1.
DR AlphaFoldDB; B2V7L9; -.
DR SMR; B2V7L9; -.
DR STRING; 436114.SYO3AOP1_0297; -.
DR PRIDE; B2V7L9; -.
DR EnsemblBacteria; ACD65942; ACD65942; SYO3AOP1_0297.
DR KEGG; sul:SYO3AOP1_0297; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
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; -; 2.
DR Gene3D; 4.10.860.120; -; 1.
DR HAMAP; MF_01322; RNApol_bact_RpoC; 1.
DR InterPro; IPR012756; DNA-dir_RpoC2_beta_pp.
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; TIGR02388; rpoC2_cyan; 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..1579
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353444"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 80
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 601
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 603
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 605
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 938
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"
FT BINDING 1019
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1022
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1579 AA; 177600 MW; 380ACF6564968A56 CRC64;
MEAKERKETV RFDAIRLSLA SPEIIRSWSH GEVKKPETLN YRTLKPEKDG LFDARIFGPI
KDYECLCGKY KKRKYEGTIC DRCGVEVTRS DVRRERFGHI ELASPVVHIW YLKSTPSKIG
SLLDLTSRDI ERVVYFESYL VIEHPTEEEE EAFEKDPKSL PLMEGGLTKY VKLHVVSEDE
FREREYEYSN AEKYEYGMGA EKVKDVLARI DLEILAKRLK KDLHGYAGTF DDLNLSYKMN
YPRLYNKAII EIARKFSEVG LRFGDIEPTE KEIDVIISQG YYIVIDPASS DLKFGQIINP
ENVDSLPEGV IALTGVEALE KLYKAYREKV KEIPIFEVIK ESVRNVILKE GTDARLKKII
RRLRLVEGFI ESENKPEWMI LEVLPVIPPD LRPLIALDGG RFASSDLNDL YRRVINRNNR
LKRLIDLDAP EIIIRNEKRM LQEAVDALID NGRRGRMVTQ NNRPLKSLSD SLRGKEGRFR
QNLLGKRVDY SGRSVIVVGP ELQMHECGLP KQMALELFKP FIYRRLEEKG YATSIKSAKK
LVEEKVPEVY ECLEEVVKQH PVLLNRAPTL HRMSVQAFEP KLVEGKAIKL HPLVCPPFNA
DFDGDQMAVH VPLSVEAQLE SYILMLSTQN ILSPAHGKPV TMPSQDIILG VHYMTQELPN
AKGEGKIFGS PEEAVTAYEL GTIDLLAKIK VRINGKIVET TAGRIIFNQI LPEGYKFVNE
VLDKKKISKL ISDIYEKYGN EIAAQTLDKI KEIGFRFATK AAVSISVADL VVPKKKAKIL
EKAIKEAETV WKQYVDGIIT KGERHNKIID IWSQATNEVA KEMFNEIEKS ERVENGKKYP
GYFNPVYMMA SSGARGSRDQ IRQLAGMRGL MAKHSGEFIE TPIMSNFREG LSVVEYFIST
YGARKGLADT ALKTAVAGYL TRRLADVAQD VIITGEDCGT LKGITVSSII ESGEIVVPFK
DRIIGRYTAE DVYDPYTGEL LISANEEITE EVVDKFEKAG IEKVKIRSVL TCEMPHGVCA
KCYGRDLAQR KLVDIGEAVG IIAAQSIGEP GTQLTMRTFH IGGAATAKEV QTQHKATHDG
TVKLQNVKFV VDKKGRKLII NREGSIKILD KEGKTIERFP APYGAVLYVE DGQEVKEGTI
LAEWEPFSDP IIAEKGGEVE LRDVILDVTL KEERDNITGK TIYTITFLRP KDAQLHTPRL
VIKGEDGNEY VYDLPVNTIL LIPKENLEEV WDKCFACSEA EKTDIHHKYL QVKKGFKVSE
GDVVAKIPKE KAKVRDIVGG LPRVEELLEA REPKNKAIIT EIDGIVKIYE DAKEITLINP
KEGKTETYKV PDTTFVIVKN GSFVKAGQSL VDDGSIVAEF DGMVRLKSEG SRIVVFNKET
GQQKDYKVPK GKFIIVKDNS VVKAGDPLTD GTPNPHDILR VMGIEELAAF LVKEAQIVYR
LQGVEINDKH FEVIIRQILR KVKIVDPGDS RFLLNEIVDK LDLEEEINKV ISEGGRPPKA
EPVLVGITKA ALTTRSWISA ASFQETTRVL ADAAVEGKVD PLKGLKENVI IGGIIPAGTG
IKEYSEVEVV LKEEEKEEV
