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RPOC_ACIAD
ID   RPOC_ACIAD              Reviewed;        1397 AA.
AC   Q6FF89;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 2.
DT   03-AUG-2022, entry version 110.
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=ACIAD0308;
OS   Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=62977;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33305 / BD413 / ADP1;
RX   PubMed=15514110; DOI=10.1093/nar/gkh910;
RA   Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA   Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA   Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT   "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT   a versatile and naturally transformation competent bacterium.";
RL   Nucleic Acids Res. 32:5766-5779(2004).
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=CAG67268.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CR543861; CAG67268.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_026056991.1; NC_005966.1.
DR   AlphaFoldDB; Q6FF89; -.
DR   SMR; Q6FF89; -.
DR   STRING; 62977.ACIAD0308; -.
DR   PRIDE; Q6FF89; -.
DR   EnsemblBacteria; CAG67268; CAG67268; ACIAD0308.
DR   GeneID; 45232822; -.
DR   KEGG; aci:ACIAD0308; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_6; -.
DR   OrthoDB; 4421at2; -.
DR   BioCyc; ASP62977:ACIAD_RS01465-MON; -.
DR   Proteomes; UP000000430; 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..1397
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000225504"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
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         467
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         469
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         819
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         893
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         900
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         903
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1397 AA;  155195 MW;  24D43E583A8B6034 CRC64;
     MKDLLDIMRK KTDSDGHTPI EFDRIRIGLA SPEMIKSWSH GEVKKPETIN YRTFKPERDG
     LFCAKIFGPV KDYECLCGKY KRMKYKGVIC EKCGVEVTTA KVRRERMGHI ELASPVAHIW
     FLKSLPSRIG LLLDMTLRDI ERVLYFESYV VTDPGMTPLE KYQLLTDEEY FNALEEHGDE
     FSAKMGAEAV QDLLKDIDLE AEISRLREEI PQTTSETKLK KASKRLKLME AFKESNNKPE
     WMVMNVLPVL PPDLRPLVPL EGGRFATSDL NDLYRRVINR NNRLKRLLDL AAPDIIVRNE
     KRMLQESVDA LLDNGRRGRA ITGSNKRPLK SLADMIKGKQ GRFRQNLLGK RVDYSGRSVI
     TVGPTLRLHQ CGLPKKMALE LFKPFIFAKL QASGQATTIK AAKKMVERET PEVWDVLANV
     IRQHPVMLNR APTLHRLGLQ AFEPILIEGK AIRLHPLVCA AFNADFDGDQ MAVHVPLTLE
     AQLEARALMM STNNILSPAN GEPIIVPSQD VVLGLYYITR DAVNAKGEGM MFADTHEVNR
     ALATGQVAIH ARVKVRVHQT VINEDGQREK QTIVVDTTPG RCLLWEVVPE GLSFEMINLE
     MTKKNISKLI NSCYRKLGLK DTVIFADQLM YLGFRQATRS GVSVGMEDMV IPPQKQAIID
     KAETEVREIE EQFEQGFVTA GERYNKVVDI WARTNDQVAK AMMDNLSFTN VKNKQGQDEK
     QKSFNSIYMM SDSGARGSAA QIRQLAGMRG LMAKPDGSII ETPIKANFRE GLTVLQYFIS
     THGARKGLAD TALKTANSGY LTRRLVDVAQ DLVITEPDCG TMGGLVMTPF IQGGDVIEPL
     RDRVLGRVTA EDVRRASDNE IVLPRGTLID EKIAAQLEEA GVDEVKVRSV IACESTFGVC
     AKCYGRDLAR GHQVNPGESV GVMAAQSIGE PGTQLTMRTF HVGGAASRTS AANSVQVRNK
     GTVRFHNVKT VQHAKGHLVS VSRSGEIGIA DELGRERERY KLPYGASILI KDGEAVEAGG
     IVATWDPHTH PLVTEVAGKA RFSQIADGVT ATSKTDDATG MTTVEILPVT ARPASGKDLR
     PAIVLDTTDG GEQFYFLPQN TIVTVRDGET IGVGDVLGRV PQETSRTRDI TGGLPRVADL
     FEARKPKEHA ILAEVSGIVS FGKETKGKNR LVITPDDGSE IYEELIPKWR TINVFEGEHV
     NRGETISDGP QNPHDILRLK GEVALTNYIV NEVQDVYRLQ GVKINDKHIE VIVRQMLRKV
     DITDGGDTSF IKGEQVDYIR VVQENQAVLA QNKFPAKFER QLMGITKASL STDSFISAAS
     FQETTRVLTE AAVTGKEDDL RGLKENVVVG RLIPAGTGLA YHLERRRQEA EAAEFELHND
     FSEVDQAFSQ ALNQEQF
 
 
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