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Entry: E6WVH6_PSEUU
LinkDB: E6WVH6_PSEUU
Original site: E6WVH6_PSEUU 
ID   E6WVH6_PSEUU            Unreviewed;      1408 AA.
AC   E6WVH6;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
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   OrderedLocusNames=Psesu_2341 {ECO:0000313|EMBL:ADV28175.1};
OS   Pseudoxanthomonas suwonensis (strain 11-1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Pseudoxanthomonas.
OX   NCBI_TaxID=743721 {ECO:0000313|EMBL:ADV28175.1, ECO:0000313|Proteomes:UP000008632};
RN   [1] {ECO:0000313|EMBL:ADV28175.1, ECO:0000313|Proteomes:UP000008632}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=11-1 {ECO:0000313|Proteomes:UP000008632};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Ovchinnikova G., Siebers A.K., Allgaier M., Thelen M.P.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Pseudoxanthomonas suwonensis 11-1.";
RL   Submitted (JAN-2011) 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|ARBA:ARBA00024550,
CC         ECO:0000256|HAMAP-Rule:MF_01322, 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}.
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DR   EMBL; CP002446; ADV28175.1; -; Genomic_DNA.
DR   RefSeq; WP_013536002.1; NC_014924.1.
DR   STRING; 743721.Psesu_2341; -.
DR   KEGG; psu:Psesu_2341; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_6; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 9815296at2; -.
DR   Proteomes; UP000008632; 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: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:UP000008632};
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   REGION          1377..1408
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: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   1408 AA;  155604 MW;  C0D0E21903D26A4E CRC64;
     MKDLLNLFNQ QRQTLDFDAI KIALASPDLI RSWSFGEVKK PETINYRTFK PERDGLFCAA
     IFGPIKDYEC LCGKYKRMKH RGVVCEKCGT EVTLAKVRRE RMGHIDLASP VAHIWFLKSL
     PSRIGLMLDM TLRDIERILY FEAFVVTEPG LTPLERRQLL TEEQYLTARQ EHGDDFDAAM
     GAEAIYELLR TIDLQAEMAR LREEIAATGS ETKLKRLTKR IKLIEAFIES GNRPEWMVMT
     VLPVLPPDLR PLVPLDGGRF ATSDLNDLYR RVINRNNRLR RLLELNAPDI IVRNEKRMLQ
     ESVDALMDNG RRGRAITGTN KRPLKSLADM IKGKQGRFRQ NLLGKRVDYS GRSVIVVGPY
     LRLHQCGLPK KMALELFKPF VFAKLQRRGL ATTIKAAKKL VEREEAEVWD ILEEVIREHP
     VLLNRAPTLH RLGIQAFEPV LIEGKAIQLH PLVCTAFNAD FDGDQMAVHV PLSLEAQLEA
     RALMMSTNNI LSPANGEPII VPSQDVVLGL YYMTRALENK KGEGMAFANV AEVKRAYDNR
     TVELHAKVKV RITEVVTDEN GNKQKKASIV DTTVGRALLA EILPAGLPFA LANTELTKKN
     ISRLINSCYR RLGLKDTVVF ADQLMYTGFS FATRAGVSIG IDDMLIPDEK KGILSEAEAE
     VLEIQEQYQS GLVTAGERYN KVVDIWSRTN ERIAKAMMET IGTDKVVNAK GEEVAQKSMN
     SLYIMADSGA RGSQAQIRQL AGMRGLMARP DGSIIETPIK ANFREGLNVQ EYFNSTHGAR
     KGLADTALKT ANSGYLTRRL VDVAQDVVIT EVDCGTIQGL TMTPIVEGGD VVEPLKDRVL
     GRVVAEDVFL PGNDEDPVVT RNTLLDEVWV NRLEEAGVQT IKVRSTITCE SAFGVCSHCY
     GRDLARGHLV NIGESVGVIA AQSIGEPGTQ LTMRTFHIGG AASRAAAVDN ITVKTTGSVK
     FTNLKSVEHA GGHLVAVSRS GEVSVLDPHG RERERYKLAY GATISVKDGA EVKAGQQIAN
     WDPHNHPIVS EVAGFVRFID FVDGITVIEK TDELTGLASR EITDPKRRGS QGKDLRPLVR
     IVDKDGNDLT IPGTDLPAQY LLPPRSIVNL QDGAPVGVGD VVAKIPQEAS KTRDITGGLP
     RVADLFEARK PKDPAILAER SGVVSFGKDT KGKQRLIIKG AEGEEHEELI PKYRQIIVFE
     GEHVTKGETI VDGEPSPQDI LRLKGIEDLA AYLVKEIQDV YRLQGVKIND KHIEVITRQM
     LRKVEITDQG DSKFLNGEQV EKQRVIEENQ RLVARNEIPA KYEPVLLGIT KASLATESFI
     SAASFQETTR VLTEAAVRGT RDSLRGLKEN VIVGRLIPAG TGLAYHSKRR RNATGLTESE
     LEALSGGSEP AAVAEVAEAA PAQDDAAE
//
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