RPOC_SHEVI
ID RPOC_SHEVI Reviewed; 1409 AA.
AC Q9KW13;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 72.
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 Shewanella violacea.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60217;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Nakasone K., Ikegami A., Sakai Y., Kato C., Horikoshi K.;
RT "Isolation of rpoB and rpoC genes from deep-sea piezophilic bacterium
RT Shewanella violacea and its overexpression in Escherichia coli.";
RL Submitted (JUL-2000) 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; AB045725; BAA99393.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KW13; -.
DR SMR; Q9KW13; -.
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; Transcription; Transferase; Zinc.
FT CHAIN 1..1409
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067790"
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"
SQ SEQUENCE 1409 AA; 155751 MW; 24C1AFF7A8546B7A CRC64;
MKDLLKFLKQ QSKTEEFNGI KIGLASPDLI RSWSFGEVKK PETINYRTFK PEREGLFCAR
IFGPVKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRE RMGHIDLASP VAHIWFLKSL
PSRIGLMLDM TLRDIERVLY FESFVVIEPG MTSLERGQML TEESYLDALE EYGDEFEAKM
GAEAVLELLR AIELEKEIES LREELPSINS ETRRKKMTKR LKLIEAFFHS GNKPEWMILK
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLAAPDI IVRNEKRMLQ
ESVDALLDNG RRGRAITGSN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVITVGPT
LRLHQCGLPK KMALELFKPF IYGKLEGRGL ATTIKAAKKM VEREVPEVWD VLDDVIREHP
VMLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCAAYNAD FDGDQMAVHV PLTLEAQLEA
RSLMMSTNNI LSPANGEPVI TPSQDVVLGL YYASRKCVNG KGEGMVFESI DEVEKAYRTG
FAAIHAQVKV RITETHIAEN GERTEARRIV DTTVGRSLLS RVLPKGLSFD LVNQNMGKKQ
IGKLLNTCYR QLGLKDTVVF ADQLMYAGFH YATVSGASVG IDDMVIPAAK YTLVADAEAE
VLEIQEQFQS GLVTAGERYN KVIDIWASAN EKISKAMMDN LSVETVINRD GEEEEQESFN
SIYMMADSGA RGSAAQIRQL AGMRGLMAKP DGSIIETPIV ANFREGLNVS QYFISTHGAR
KGLADTALKT ANSGYLTRRL VDVAQDLVVI EDDCGTFEGL TMKPLIEGGD VVEPLRERVL
GRVVALDVFY PGTEKVLAPR NTLLDEAWCD TLEDNSIDEV IVRSVISCNT DFGVCKACYG
RDLARGHIIN QGEAIGVVAA QSIGEPGTQL NGWRTFHIGG AASRASAENN VQVKNAGTVK
LHNAKHVTNS EGKLVIVSRS SEVAIIDELG REKERYKVPY GTILEKLEES IVTAGEIIAN
WDPHTHPIIS EVAGTIKFVD MIEGVTMTRQ TDDLTGLSSI VVMEVGQRPT AGKEMRPSIR
LLDASGEDLK IPGTEVPAQY FLPGKAIVNQ DDNAEINVGD ALARIPQESS KTRDITGGLP
RVADLFEARK PKEPAILAEY SGTISFGKET KGKRRLLITP ADGGKPYEEM IPKWRNLNVF
EGEKVERGEV IADGAEAAHD ILRLRGIHKV ANYIVNEVQD VYRLQGVKIN DKHIEVIIRQ
MLRKCLITDA GDSQFLAGEQ AEVARVKIAN RELEAQGKKP ATFDRELLGI TKASLATESF
ISAASFQETT RVLTEAAVGG KSDKLRGLKE NVIVGRLIPA GTGYAYHQKR NAALAAKASG
KTSEQATTIT ASEAERNLAD LLNLAGSSD
