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Database: UniProt
Entry: A0A0Q8ETL8_9GAMM
LinkDB: A0A0Q8ETL8_9GAMM
Original site: A0A0Q8ETL8_9GAMM 
ID   A0A0Q8ETL8_9GAMM        Unreviewed;      1410 AA.
AC   A0A0Q8ETL8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=DNA-directed RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE            Short=RNAP subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE            EC=2.7.7.6 {ECO:0000256|HAMAP-Rule:MF_01322};
DE   AltName: Full=RNA polymerase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
DE   AltName: Full=Transcriptase subunit beta' {ECO:0000256|HAMAP-Rule:MF_01322};
GN   Name=rpoC {ECO:0000256|HAMAP-Rule:MF_01322};
GN   ORFNames=ASD77_17575 {ECO:0000313|EMBL:KRA50539.1};
OS   Pseudoxanthomonas sp. Root65.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=1736576 {ECO:0000313|EMBL:KRA50539.1, ECO:0000313|Proteomes:UP000051430};
RN   [1] {ECO:0000313|EMBL:KRA50539.1, ECO:0000313|Proteomes:UP000051430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root65 {ECO:0000313|EMBL:KRA50539.1,
RC   ECO:0000313|Proteomes:UP000051430};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA50539.1, ECO:0000313|Proteomes:UP000051430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root65 {ECO:0000313|EMBL:KRA50539.1,
RC   ECO:0000313|Proteomes:UP000051430};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
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:0000256|HAMAP-Rule:MF_01322,
CC         ECO:0000256|RuleBase:RU004279};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_01322};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01322};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_01322}.
CC   -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC       {ECO:0000256|HAMAP-Rule:MF_01322, ECO:0000256|RuleBase:RU004279}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRA50539.1}.
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DR   EMBL; LMHA01000005; KRA50539.1; -; Genomic_DNA.
DR   RefSeq; WP_055945219.1; NZ_LMHA01000005.1.
DR   STRING; 1736576.ASD77_17575; -.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000051430; Unassembled WGS sequence.
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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR   CDD; cd02655; RNAP_beta'_C; 1.
DR   CDD; cd01609; RNAP_beta'_N; 1.
DR   Gene3D; 1.10.132.30; -; 1.
DR   Gene3D; 1.10.150.390; -; 1.
DR   Gene3D; 1.10.1790.20; -; 1.
DR   Gene3D; 1.10.40.90; -; 1.
DR   Gene3D; 2.40.40.20; -; 1.
DR   Gene3D; 2.40.50.100; -; 3.
DR   Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR   Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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   NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR   PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR   PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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   SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
PE   3: Inferred from homology;
KW   DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW   ECO:0000256|HAMAP-Rule:MF_01322};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01322};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_01322}; Reference proteome {ECO:0000313|Proteomes:UP000051430};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW   Rule:MF_01322};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_01322}; Zinc {ECO:0000256|HAMAP-Rule:MF_01322}.
FT   DOMAIN          235..514
FT                   /note="RNA polymerase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00663"
FT   BINDING         70
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         72
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         85
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         462
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         464
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         814
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         889
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         896
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
FT   BINDING         899
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1410 AA;  155271 MW;  3401D159490FA976 CRC64;
     MKDLLNLFNQ QRQTLDFDAI KIALASPDLI RSWSFGEVKK PETINYRTFK PERDGLFCSA
     IFGPIKDYEC LCGKYKRMKH RGVVCEKCGT EVTLAKVRRE RMGHIDLASP VAHIWFLKSL
     PSRIGLMLDM TLRDIERVLY FEAYVVTEPG LTSLERRQLL TEEQFMQARQ EHGDDFDAAM
     GAEAVYDLLR TIDLQAEMVN LREDIASTGS ETKLKRLTKR IKLMEAFLES GNRPEWMVMT
     VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLR RLLELNAPDI IVRNEKRMLQ
     ESVDALMDNG RRGRAITGTN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVIVVGPT
     LRLHECGLPK KMALELFKPF VFAKLQRRGL ATTIKAAKKL VEREEADVWD ILEEVIREHP
     VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHV PLSLEAQLEA
     RALMMSSNNI LSPANGEPII VPSQDVVLGL YYMTRALENK KGEGMAFANI AEVKRAYDNR
     AVELHAKVKV RISGTVIDED GGRSQQSSIV DTTIGRALLA EILPEGLPFA LVNTELNKKA
     ISRLINSSYR MLGLKDTVVF ADKLMYTGFA YATRAGVSIG IDDMLIPAEK KGILGEAEQE
     VLEIQEQYQS GLVTAGERYN KVVDIWSRTN ERIAKAMMDT IGTDKVQNAK GETINEKSMN
     SLYIMADSGA RGSQAQIRQL AGMRGLMARP DGSIIETPIK ANFREGLNVQ EYFNSTHGAR
     KGLADTALKT ANSGYLTRRL VDVAQDVVIT EVDCGGNEGL TMTPIVEGGD VVEPLRDRVL
     GRIVAEDVFL PGNDEDPIVT RNTLLDEAWV QKLEDAGVQA LKVRSTITCE STFGVCAHCY
     GRDLARGHIV NIGEAVGVIA AQSIGEPGTQ LTMRTFHIGG AASRAAAVDN ITVKTTGSIK
     FNNLKFVEHA NGSLVAVSRS GELSVLDGHG RERERYKLPY GATINVKDGA QITAGQAVAN
     WDPHNHPIVS EVAGFVRFVD FVDGVTVIEK TDDLTGLASR EITDPKRRGS QGKDLRPIVR
     IVDKDGKDLS IPGTDLPAQY LLPPRSIVNL QDGAPVGVGD VVTKVPQEAS KTRDITGGLP
     RVADLFEARK PKDPAILAER SGVISFGKDT KGKQRLIIKD TDGSEHEELI PKFRQIIVFE
     GEHVAKGETI VDGEPSPQDI LRLLGVEPLA AYLVKEIQDV YRLQGVKIND KHIEVITRQM
     LRKVEITDAG NSKFLAGEQI EKQRFIEENA KLIARNELPA KYDPVLLGIT KASLATESFI
     SAASFQETTR VLTEAAVRGT RDSLRGLKEN VIVGRLIPAG TGLAYHNQRR RNASGLTEAE
     VNALSGGVAE AAPAAAVATT DEAGEESSAS
//
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