RPOC_COXBN
ID RPOC_COXBN Reviewed; 1414 AA.
AC A9KD37;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=CBUD_1860;
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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; CP000733; ABS77749.1; -; Genomic_DNA.
DR RefSeq; WP_011997293.1; NC_009727.1.
DR AlphaFoldDB; A9KD37; -.
DR SMR; A9KD37; -.
DR EnsemblBacteria; ABS77749; ABS77749; CBUD_1860.
DR KEGG; cbd:CBUD_1860; -.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008555; 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; 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; Zinc.
FT CHAIN 1..1414
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353341"
FT REGION 1392..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 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 1414 AA; 157176 MW; A4B8167C4577799D CRC64;
MRDLVKQLKS EKHTAEFDAL RIKLASPEEV RSWSYGEVKK PETINYRTFK PEREGLFCAK
IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTLAKVRRE RMGHIELASP VAHIWYLKSL
PSRIGLLLDV TLRDIERILY FEAYVVVDPG MTDLEPRQLL SEEAYLDALE EYGDDFTALM
GAEAIQRLLR DIDVEAEVEA LRTELQTTTS ETKTKKLTKR LKVLSAFLES GNKPEWMILT
VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLK RLLDLNAPDI IVRNEKRMLQ
EAVDALLDNG RRGRAILGSN RRQLKSLADM IKGKSGRFRQ NLLGKRVDYS GRSVIVVGPT
LKLHQAGLPK KMALELFKPF IFSKLQLRGL ATTVKAAKKL VENEGPEVWD ILEEVIREHP
ILLNRAPTLH RLGIQAFEPV LVEGKAIQLH PLVCTAYNAD FDGDQMAVHV PLTLEAQLEA
RSLMMSTNNV LHPANGEPII VPSQDVVLGL YYITRDRVNA KGEGMRFADA QEVVRAYEND
QVDLHARITV RIKEGILNEA GEIEESDRLV NTAAGRILLW QIVPKGLPFA LVDQPMTKKA
VTKLLDFCYR NLGLKTTVIF ADKLMYMGFH YATHSGVSIG INDLVVPDQK EAIISRAEDE
VREIEKQYAS GLVTHGERRN KVIDIWSRTN DQVAKAMMEK IAVEKVKDAE GKEVAQSSFN
SIYMMSDSGA RGSAAQTRQL AGMRGLMARP DGTIIETPIT ANFREGLNVL QYFISTHGAR
KGLADTALKT ANSGYLTRRL VDVAQDLVVT EHDCGTEASI EMMPHIEGGD VVEPLRERVL
GRILAEPVMD PKSRKELLAK DTFLDERRVD ILEEHSIDRV RVRSAITCEA RYGICSMCYG
RDLARGHVVN VGEAIGVVAA QSIGEPGTQL TMRTFHIGGA ASRATAANNI EVKSTGKIKL
RNLKTVEQAQ GNLVAVSRSG ELVVQDLQGS EREHYKVPYG ATISVRDGDS VKAGQIVAQW
DPHTHPIITE VAGTLRFVDL VDGVTMNRQT DELTGLSSIV ITSTKQRSAS GKELRPMVKL
VDKNDDDLFL PGGKVPAHYF LPEGTFLTKE DGTTVNIGDV LARIPQETSK TRDITGGLPR
VADLFEARRP KDAAILAEIS GVVSFGKDTK DKGRLIITAP DGTTHEELIP KWRHVSVFEG
ETVEKGEVIA DGPRDPHDIL RLLGVNALAN YIVNEVQEVY RLQGVKINDK HIEVIVRQML
RKVKITQPGD TDLLQNEQVE RTRVREENEK IIKKDGTVAK VEPILLGITK ASLATESFIS
AASFQETTRV LTAASVAGKR DDLRGLKENV IVGRLIPAGT GFSYHQQRRA VAGKSVEEKE
IEEKRVTASE AEQALSEALK SSAPQEAKAA QKDE
