RPOC_JANMA
ID RPOC_JANMA Reviewed; 1414 AA.
AC A6T3L2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=mma_3419;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR89599.1; -; Genomic_DNA.
DR RefSeq; WP_012081256.1; NC_009659.1.
DR AlphaFoldDB; A6T3L2; -.
DR SMR; A6T3L2; -.
DR STRING; 375286.mma_3419; -.
DR PRIDE; A6T3L2; -.
DR EnsemblBacteria; ABR89599; ABR89599; mma_3419.
DR KEGG; mms:mma_3419; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; JSP375286:MMA_RS17670-MON; -.
DR Proteomes; UP000006388; 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; 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..1414
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308838"
FT REGION 1395..1414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 815
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 889
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 896
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 899
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1414 AA; 156122 MW; 9977E109212F61D5 CRC64;
MKALLDLFKQ VQQNEQFDAI KIGLASPEKI RSWSYGEVKK PETINYRTFK PERDGLFCAK
IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTLAKVRRE RMGHIELASP TAHIWFLKSL
PSRLGMVLDM TLRDIERVLY FEAYVVTDPG MTPLKKCQIM SEDDYAAKYE EFGDDFTAFM
GAEGIRELLR AIDIDRDAEM LRQELKDSKS EAKIKKYAKR LKVLEAFQRS GIKPDWMIME
VLPVLPPELR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLMELRAPEI ITRNEKRMLQ
EAVDSLLDNG RRGKAMTGAN KRPLKSLAEM IKGKGGRFRQ NLLGKRVDYS GRSVIVVGPQ
LKLHQCGLPK LMALELFKPF IFNKLELMGL ATTIKAAKKL VEIQEPVVWD ILEDVIREHP
VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAFNAD FDGDQMAVHV PLSIEAQMEA
RTLMLASNNI LFPSNGEPSI VPSQDIVLGL YYASREAINA KGEGMMFPDV SEVIRAYDNK
MVELATRITV RITEYPKNVE TGEFEKTVTR YETTVGRAIL SEILPKGLPF SVLNRALKKK
EISRLINLSF RKCGLRATVV FADQLLQSGF RLATRAGISI CVDDMLVPKQ KVDIIATAES
EVKQIEQQYS SGLVTAGERY NKVVDIWGKA GDDVGKAMMD QLKVEDVTKR DGTKTTQESF
NAIYMMADSG ARGSAAQIRQ LAGMRGLMAK PDGSIIETPI TANFREGLNV LQYFISTHGA
RKGLADTALK TANSGYLTRR LVDVTQDLVV IEDDCGTSNG ASMKALVEGG EVIEALRDRI
LGRVAANDIV NPETQATLYA AGTLLDEDMV EEIERLGIDE VKVRTPLTCD TRFGLCAQCY
GRDLGRGTLV NAGEAVGVVA AQSIGEPGTQ LTMRTFHIGG AASRAAVASS VEAKSNGTVR
FTATMRYVTN GKGGQIVISR SGEVLITDDH GRERERHKVP YGATLIVKDG MVIKAGTALA
TWDPLTRPII TEYTGTVKFE NVEEGSTVAR QIDEVTGLST LVVIDAKRRG SVTKTVRPQV
KLLNEQGEEV KIAGTEHAVT IGFQVGALIT VKDGQQVTVG EVLARIPTES QKTRDITGGL
PRVAELFEAR SPKDAGMLAE VTGTVAFGKE TKGKQRLEIT DMDGNKHEFL ITKDKQVLVH
DGQVVNKGEM IVDGPADPQD ILRLLGIEAL ARYIVDEVQD VYRLQGVKIN DKHIEVIVRQ
MLRRVQVVDA GDANYIVGEQ VERSELLDEN DRVIALGKIP ATYENVLLGI TKASLSTDSF
ISAASFQETT RVLTEAAIMG KKDGLRGLKE NVIVGRLIPA GTGLAFHRAR KEKDSWEAEE
RAALLQSEKA ARAAEAEAQF ADVSSTPDSD TDAS
