RPOC_RHOCS
ID RPOC_RHOCS Reviewed; 1430 AA.
AC B6IRP7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=RC1_0702;
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW;
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000613; ACI98133.1; -; Genomic_DNA.
DR RefSeq; WP_012565925.1; NC_011420.2.
DR AlphaFoldDB; B6IRP7; -.
DR SMR; B6IRP7; -.
DR STRING; 414684.RC1_0702; -.
DR PRIDE; B6IRP7; -.
DR EnsemblBacteria; ACI98133; ACI98133; RC1_0702.
DR KEGG; rce:RC1_0702; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001591; 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 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..1430
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141790"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 495
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 497
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 838
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 912
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 919
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 922
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1430 AA; 159414 MW; 8016ECC63674DA61 CRC64;
MNELMNIFGQ PQGPQSFDQI RISIASPERI RSWSFGEIKK PETINYRTFK PERDGLFCAR
IFGPIKDYEC LCGKYKRMKY RGIICEKCGV EVTLSKVRRE RMGHIELASP VAHIWFLKSL
PSRIGLLLDM TLKDLERILY FENYVVIEPG LTDLKLHELL SEDQLLDKQD KFGEDAFTAK
IGAEAMKDLL ANLDLIEEKA TCREELKETA SEAKRKKLVK RLKLIEAFLG PSQEVEDVAA
YERFEGYKER IERPDARPLF KIFPDATRPE WMILEVVPVI PPELRPLVPL DGGRFATSDL
NDLYRRVINR NNRLKRLIEL KAPDIIVRNE KRMLQEAVDA LFDNGRRGRV ITGANKRPLK
SISDMLKGKQ GRFRQNLLGK RVDYSGRSVI VVGPELKLHQ CGLPKKMALE LFKPFIYAKL
ELYGLASTIK AAKRMVEKER PEVWDILEEV IREHPVMLNR APTLHRLGIQ AFEPTLIEGK
AIQLHPLVCT AFNADFDGDQ MAVHVPLSLE AQLEARVLMM STNNILSPAS GRPIIVPSQD
IVLGLYYITM ELPGMVGEGM AFGTIGEIEH ALASKAVSLH AKIQCRYKTV DDEGNPITVR
VTTTPGRMLL SEILPRHKAI KFDLINRLLT KKEIGNIIDV VYRHCGQKET VIFADRLMKL
GFSNAFKAGI SFGKDDMVIP AEKEILIREA QDRVKEYEQQ YLDGLITQGE KYNKVVDVWS
ETTEKVASAM MKVIEQPKPG FGVNSVYMMA HSGARGSAAQ IKQLAGMRGL MAKPSGEIIE
TPIISNFKEG LTVLEYFNST HGARKGLADT ALKTANSGYL TRRLVDVAQD AIIVENDCGT
TRGITMKAVI DGGEIVVPLG ERILGRTVSV DIIHPLTGEM LVAAGDMITE REVEVIERAG
IDSVHIRSVL TCETRDGVCA QCYGRDLARG TRVNMGEAVG VIAAQSIGEP GTQLTMRTFH
IGGAAQRGAE QSFIEATLDA KVMVKNRNLV MNSEGVPVVM GRNCELALLD EQGRERARHR
VPYGAKLNKA LAADGAMIKK GDRLAEWDPY TLPILTEREG IANYVDLVEG VSVREVVDEA
TGISSKVVTD WRQQPRGADL RPRITLRDET GEVVKLPNGL EARYYMSVDA ILSVENGARV
RAGDVLARIP RESSKTRDIT GGLPRVAELF EARRPKDFAI ISDIDGRVEF GKDYKTKRRI
VVRNDETGEE KEYLIPKGKH ISVQEGDYVQ KGDLLMDGNP VPHDILAVMG VESLANYLIN
EIQDVYRLQG VKINDKHIEV IVRQMLQKVE ITDPGDTTLL AGEQVDRTEF EEENRLVQQR
MNEGEQDLRF AIAKPVLQGI TKASLQTRSF ISAASFQETT RVLTEAAVQG KVDNLEGLKE
NVIVGRLIPA GTGSVVNRLK QIAAERDKAL QLADGVDETP ALADGGEAAA
