RPOC_GLUOX
ID RPOC_GLUOX Reviewed; 1439 AA.
AC Q5FTX8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=GOX0385;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000009; AAW60168.1; -; Genomic_DNA.
DR RefSeq; WP_011251970.1; NZ_LT900338.1.
DR AlphaFoldDB; Q5FTX8; -.
DR SMR; Q5FTX8; -.
DR STRING; 290633.GOX0385; -.
DR PRIDE; Q5FTX8; -.
DR EnsemblBacteria; AAW60168; AAW60168; GOX0385.
DR KEGG; gox:GOX0385; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000006375; 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; -; 2.
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..1439
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225539"
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 504
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 506
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 508
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 862
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 936
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 943
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 946
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1439 AA; 159527 MW; 4158FD2BB21A4C35 CRC64;
MNELMKILGQ TGQSVTFDQI KIQLASSEQV RSWSYGEIKK PETINYRTFK PERDGLFCAR
IFGPIKDYEC LCGKYKRMKF RGIVCEKCGV EVTLAKVRRE RMGHIELASP VAHIWFLKSL
PSRIATMLDL PLKDVEPVLY FEKFLVLDKG VCESDQIDSY KNGKKRDQYL LDEIRCEDLL
DEYPDAGIDV GIGAEAIKRA LSSYDWGIPN DQERELSLAA KEKGLPDPFD YDADVMEGDS
EKTMMRKKLR KATSEAARKK LVKRLKLVEA FVESGSRPDW MIMDIVPVIP PELRPLVPLD
GGRFATSDLN DLYRRVINRN NRLKRLIELR APDIIVRNEK RMLQEAVDAL FDNGRRGRAI
TGANKRPLKS LSDMLKGKQG RFRQNLLGKR VDYSGRSVIV VGPELKLHQC GLPKKMALEL
FKPFIYSKLE KYGHATTIKA AKRMVEKERP EVWDILEEVI REHPVMLNRA PTLHRLGIQA
FEPTLIEGKA IQLHPLVCTA FNADFDGDQM AVHVPLSLEA QLEARVLMMS TNNILSPANG
KPIIVPSQDI VLGLYYLSLE VPEYRETPDE AVIKDGKIVT AAPPAYSDVA EIESAMLSGS
LKLHDKIRLR LPTIDAEGKS VRQTILTTPG RALIAQILPK HQAIPFSLVN KQLTKKNVSD
VIDTVYRHCG QKEAVIFCDR LMGLGFRHAA RAGISFGKDD MIIPEAKATL VGKTSEEVKE
FEQQYQDGLI TAGERYNKVV DAWSRCTDEV QAAMLKEISK QVIGKPTNSV WMMSHSGARG
SPAQMKQLAG MRGLMVKPSG EIIEQPIIAN FKEGLSVLDY FTSSHGARKG LADTALKTAN
SGYLTRRLVD VAQDCIIVEP DCGTERGLTV RAVMDSGEVV ASLSERILGR TLSKDVIHPV
TQDVILPRNT LIEEAEAELI EKAGVESVDI RSVLTCDSRV GICAHCYGRD LARGTPVNIG
EAVGVIAAQS IGEPGTQLTM RTFHIGGAAT RGAEQSMVEA SRDGIVTIKN RNVVENSQKV
LVVMSRNCEI LLTDENGVER ARYRVPYGAR LMVSEGEAVT RTQKMAEWDP YTLPIITEQA
GTVEYLDLID SITLVERMDE VTGLSSKVVV DYKQAAKGVD LRPRLQLKDA SGNVVKLANG
NDARYFLSPD SILSVENGAE VNAGDVLARI PREGSKTRDI TGGLPRVAEL FEARRPKDHA
IIAEGEGRIE FGKDYKSKRC VIVKNDDTGE ETQYLIPKGK HVSVQEGDFV QKGDPLVDGP
RVPHDILKVM GVEALSDYLV NEIQDVYRLQ GVKINDKHIE VIVRQMLQKV EILEPGDSTY
LIGETVDRIE YEGENQRLME NGDTPAKAMP VLQGITKASL QTQSFISAAS FQETTRVLTD
AATSGKVDTL NGLKENVIVG RLIPAGTGSV MNRLRSIAAS QDRQRVGGAS PKAVEDAAE
