RPOC_LEUPS
ID RPOC_LEUPS Reviewed; 989 AA.
AC P94899;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000305};
DE Short=RNAP subunit beta';
DE EC=2.7.7.6;
DE AltName: Full=RNA polymerase subunit beta';
DE AltName: Full=Transcriptase subunit beta';
DE Flags: Fragment;
GN Name=rpoC;
OS Leuconostoc pseudomesenteroides.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=33968;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12291 / DSM 20193 / JCM 696 / NCDO 768 / NCIMB 8699 / NCFB 768
RC / 39;
RX PubMed=8863429; DOI=10.1099/00207713-46-4-1004;
RA Morse R., Collins M.D., O'Hanlon K., Wallbanks S., Richardson P.T.;
RT "Analysis of the beta' subunit of DNA-dependent RNA polymerase does not
RT support the hypothesis inferred from 16S rRNA analysis that Oenococcus oeni
RT (formerly Leuconostoc oenos) is a tachytelic (fast-evolving) bacterium.";
RL Int. J. Syst. Bacteriol. 46:1004-1009(1996).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000250}.
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:0000250|UniProtKB:P0A8T7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P0A8T7};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P0A8T7};
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 (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000305}.
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DR EMBL; X95812; CAA65079.1; -; Genomic_DNA.
DR AlphaFoldDB; P94899; -.
DR SMR; P94899; -.
DR STRING; 1154757.Q5C_06750; -.
DR eggNOG; COG0086; Bacteria.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.274.100; -; 1.
DR Gene3D; 4.10.860.120; -; 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; 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 TIGRFAMs; TIGR02386; rpoC_TIGR; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase.
FT CHAIN <1..>989
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067753"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT BINDING 387
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P0A8T7"
FT NON_TER 1
FT NON_TER 989
SQ SEQUENCE 989 AA; 109915 MW; 55B1CD8CA8739D06 CRC64;
RIRYKGIVCD RCGVEVTSSK VRRERMGHIE LAAPVTHIWY FKGIPSRMGL VLDMSPRSLE
EIIYFASYVV IEPGDAPVEK KQMVTEREYR QLKKEYGAGF KAGMGAEAIK ELLANVDLAG
ERDELKRELQ EATGQKRVRA VRRLDIVEAF LQSDNKPEWM VMDVVPVIPP DLRPMVQLEG
GRFATSDLND LYRRVINRNN RLKRLLDLNA PGIIVQNEKR MLQEAVDALI DNGRRGRPVA
GPGNRPLKSL SHMLKGKQGR FRQNLLGKRV DYSGRSVIDV GPFLKMNQMG LPVPMAIELF
RPFIMKELTT RKLAGNVKSA KRKIDKADGD VMDVLEDVIK EHPVLLNRAP TLHRLGIQAF
EPVLVSGKAM RLHPLVTEAY NADFDGDQMA IHVPLSDEAQ AEARLLMLAA GHILAPKDGK
PIVAPSQDMV IGNYYLTTEE AGREGEGMIF SGVDEARIAF ARKVVHYHTR VGIQTSSFPA
EKPFTDEQRS KVMVTSVGKL IFNEILPTDF PFINEPSEDN FKGVDDRFFI ESGEDIHDYL
AETPIIGAFK KGFLSDIIAE VYKRYKVTET SLLLDRMKDL GYEKSTESGL TVAMTDVTDL
KEKPAILEDA HNQVATVTKQ FRRGLITDDE RYQRVTEIWT KAKDIIQDKL IESFEPTNPI
FMMQDSGARG NISNFVQLAG MRGLMAGPGG KIIELPVTAN FREGLTVMEM FISTHGARKG
MSDTALKTAN SGYLTRRLVD VAQDVIVREF DNDSDRGVAV KAIMDGTSVV EPLYDRILGR
YAMKSVFDPE TGEKIVSRNE MIDEDVAKAI VNAGIEEVTI RSVFTSTTEH GVSVLDYGRN
LASGEEVEVG EAVGTVAAQS IGEPGTQLTM RNFHTGGVAG GNDITQGLPR VQEIVEARIP
KGRAEISEVT GVVTAIEENP AERTKAVTIE GETDTRTYTL PLTARMRFAE GDEIQRGDAI
NEGPIDPKEL LAVTDTLTTE SYMLTEIQK
