RPOC_PSEPU
ID RPOC_PSEPU Reviewed; 1398 AA.
AC P19176;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 3.
DT 03-AUG-2022, entry version 92.
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};
OS Pseudomonas putida (Arthrobacter siderocapsulatus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=303;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Danilkovich A.V., Borodin A.M., Allikmets R.L., Rostapshov V.M.,
RA Chernov I.P., Azhikina T.L., Monastyrskaya G.S., Sverdlov E.D.;
RT "Nucleotide sequence of the rpoC gene coding for the beta'-subunit of RNA
RT polymerase in Pseudomonas putida.";
RL Dokl. Biochem. 303:241-245(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-497.
RX PubMed=3219133;
RA Borodin A.M., Danilkovich A.V., Chernov I.P., Azhykina T.L.,
RA Rostapshov V.M., Monastyrskaya G.S.;
RT "Genes coding for RNA polymerase in bacteria. III. The use of modified
RT Sanger's method for sequencing the C-terminal region of rpoB gene, N-
RT terminal region of rpoC gene and intercistron region of RNA polymerase in
RT Pseudomonas putida.";
RL Bioorg. Khim. 14:1179-1182(1988).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25987.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA34538.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X16538; CAA34538.1; ALT_INIT; Genomic_DNA.
DR EMBL; M38319; AAA25987.1; ALT_INIT; Genomic_DNA.
DR PIR; JN0420; JN0420.
DR AlphaFoldDB; P19176; -.
DR SMR; P19176; -.
DR STRING; 1240350.AMZE01000092_gene670; -.
DR PRIDE; P19176; -.
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: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; Transcription; Transferase; Zinc.
FT CHAIN 1..1398
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067779"
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 814
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 888
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT CONFLICT 6
FT /note="N -> I (in Ref. 2; AAA25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="L -> V (in Ref. 2; AAA25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 192
FT /note="I -> T (in Ref. 2; AAA25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 317
FT /note="I -> T (in Ref. 2; AAA25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 324
FT /note="L -> S (in Ref. 2; AAA25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="L -> R (in Ref. 2; AAA25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 471
FT /note="P -> L (in Ref. 2; AAA25987)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="T -> I (in Ref. 2; AAA25987)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1398 AA; 153546 MW; 2C134F17FC2899C9 CRC64;
MKDLLNLLKN QGQVEEFDAI RIGLASPEMI RSWSFGEVKK PETINYRTFK PERDGLFCAK
IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVALGKVAAE RMGHIELACG LAHIWFLKSL
PSRIGLLMDM TLRDIERVLY FESYVVIDPG MTTLEKGQLL NDEQYFEALE EFGDDFDAAM
GAEAVRELLH AIDLEHEIGP LREEIPQTNS ETKIKKLSKR LKLMEAFQGI GNLPEWMVLT
VLPVVPAPLG PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RQLDLSAPDI IVRNEKPMLQ
EAVEPLLDNG ACGVAIIGSN KRPLKSLADM IKGKQGLFRQ NLLGKRVDYS GRSVISVGPT
LRLHQCGLPK KMALELFKPF IFGKLEMRGL ATTIKAAKKM VERELPEVWD VLAEVIREHP
VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCARYNAD FDGDQMAVDV PLTLEAQLEN
GALMMSTNNI LSPANGEPII VPSQDVVLGL YYMTREAINA KGEGRVFADL QEVDRVFRAG
EAALHAKIKV RINETVKERD GSVVKNTRIV DTTVGRALLF QVVPGGLPYD VVNQPMKKKA
ISKLINQCYR VVGLKETVIF ADQLMYTGFA YSTISGVSIG VNDFVIPDEK ARIIGNATDE
VKEIESQYAS GLVTQGEKYN KVIDLWSKAN DEVSKAMMAN LSKEKVIDRE GKEVEQESFN
SMYMMADSGA GGSAAQIRQL AGMRGLMAKP DGSIIETPIT ANFREGLSVL QYFISTHGAR
KGLADTALKT ANSGYLTRRL VDVAQDLVVT EIDCGTDQGL VMTPHIEGGD VVEPLGERVL
GRVIARDVFK PGTEDVIVPA GTLVDEQWVE FIELNSIDEV IVRSPINCET RYGICAKCYG
RDLARGHQVN IGEAVGVIAA QSIGEPGTQL TMRTFHIGGA ASRTSAADSV QVKNGGMGAS
RNLKQVERAD GNLVAVSRSG ELAIADEFGR ECEYKLPYGA VISVKEGEKV EAGAIVAKWD
PHTHPIVTEL KGTVTFVGME ENITIKRQTD ELTGLTNIEV LDVKDRPAAR RHTLRPAIKM
VDAAGKDLYL PGTDVPAQYF LPANALVGVA DGAQIGVGDV IARIPQETSK TRDITGGLPR
VADLFEARRP KEASILAEVS GTIAFGKETK GKRRLVITPT DGSEPYEELI PKWRHLNVFE
GEQVNRGEVI SDGPSDPDDI LRLLGVSALG KYIDNEIQDV YRLQGVKIND KHIETILRQM
LRKVRISESG DSSFIKGDQM EYPGAGRERA SASEDKFISK FTRVLLGITK ASLSTESFIS
AASFQETTRV LTEAAVTGKR DYLRGLKENV VVGRLIPAGT GLAYHTERMA RRDADKPLRV
SASEVEAALT EALNSSGN
