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RPOC_ACTP2
ID   RPOC_ACTP2              Reviewed;        1412 AA.
AC   A3N326;
DT   04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=APL_1728;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN74812.1; -; Genomic_DNA.
DR   RefSeq; WP_011848649.1; NC_009053.1.
DR   AlphaFoldDB; A3N326; -.
DR   SMR; A3N326; -.
DR   STRING; 416269.APL_1728; -.
DR   PRIDE; A3N326; -.
DR   EnsemblBacteria; ABN74812; ABN74812; APL_1728.
DR   KEGG; apl:APL_1728; -.
DR   PATRIC; fig|416269.6.peg.1797; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_6; -.
DR   OMA; YRNIRVE; -.
DR   Proteomes; UP000001432; 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..1412
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000353277"
FT   BINDING         71
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         73
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         86
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         461
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         463
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         465
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   1412 AA;  156762 MW;  36A3F8DADCE161F4 CRC64;
     MKDLVKFLKA QSKSNDDFDV IKIGLASPDK IRSWSFGEVK KPETINYRTF KPERDGLFCA
     RIFGPVKDYE CLCGKYKRLR HRGVICEKCG VEVTQTKVRR DRMGHIELAC PVAHIWFLKS
     LPSRIGLILD MPLRDIERVL YFESYVVTEP GMTDLEKNQL LTEEQFLDAE ERWGDEFEAK
     MGAEGIQALL RDMDLEHQCE MMREELQETN SETKRKKITK RLKLLEAFQQ SGNKPEWMVM
     TVLPVLPPDL RPLVPLDGGR FATSDLNDLY RRVINRNNRL KRLLDLVAPD IIVRNEKRML
     QESVDALLDN GRRGRAITGS NKRPLKSLAD MIKGKQGRFR QNLLGKRVDY SGRSVITVGP
     YLHLHQCGLP KKMALELFRP FIYSKLESRG IASTIKAAKK MVEREEPIVW DILAEVIREH
     PILLNRAPTL HRLGIQAFEP ILIEGKAIQL HPLVCAAFNA DFDGDQMAVH VPLTLEAQLE
     ARALMMSTNN VLSPASGDPI IVPSQDVVLG LYYMTREKVN AKGEGMYFLD PREAEKAYRT
     GQAELHARVK VRITEHVKNE AGELVAETKL LDTTIGRAIL WMIAPKGMPF KVFNQTLGKK
     AISKLINESY RRLGLKESVI LADQIMYTGF AYAARSGASV GIDDMVIPAQ KHEIIRAAEA
     EVAEIQEQFN SGLVTAGERY NKVIDIWAAA NERVAKAMME NLSTEEVINR EGNPEKQASF
     NSIFMMADSG ARGSAAQIRQ LAGMRGLMAR PDGSIIETPI TANFREGLNV LQYFISTHGA
     RKGLADTALK TANSGYLTRR LVDVAQDLVI TEDDCGTHEG IVMTPLIEGG DVKEALRDRV
     LGRVVAEDVL KPGTEEVLIP RNTLIDEKWC DVIDAESVDV IKVRSVVTCN TDFGVCAKCY
     GRDLARGHLI NQGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASAAAKESS IQVKNAGTIK
     LTNAKFVTNK EGKIVLTSRN TELTVIDTFG RTKENYKVPY GAVLSKNDGA EVAVGEVVAN
     WDPHTMPVIS EVSGRIQFSD IVDGLTVTRQ TDELTGLSSI VVQDVGERAT AGKDLRPALR
     LVDAQGNDIL IPSTDVAAQY FLPGKAIVTL DDGAEIEVGE ALARIPQESV GTKDITGGLP
     RVADLFEARK PKEPAILAEI SGIVSFGKET KGKRRLVITP AEGEAFEEMI PKWRQLNVFE
     GEMVQRGDVI SDGAETPHDI LRLRGVHAVT DYIVNEVQEV YRLQGVKIND KHIEVIVRQM
     LRKAVITNAY DSEFLEGEQV EVSRVKIANR KRAEEGKPLV EFERELLGIT KASLATESFI
     SAASFQETTR VLTEAAVAGK RDELRGLKEN VIVGRLIPAG TGFAYHQNRA KKRNQQEQAV
     AFEAPVEKLT GSQPMLISKR NSNSLQTMQL KA
 
 
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