RPOC_CHLL3
ID RPOC_CHLL3 Reviewed; 1498 AA.
AC Q3B1H8;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Plut_1961;
OS Chlorobium luteolum (strain DSM 273 / BCRC 81028 / 2530) (Pelodictyon
OS luteolum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=319225;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 273 / BCRC 81028 / 2530;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelodictyon luteolum DSM 273.";
RL Submitted (AUG-2005) 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: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; CP000096; ABB24803.1; -; Genomic_DNA.
DR RefSeq; WP_011358673.1; NC_007512.1.
DR AlphaFoldDB; Q3B1H8; -.
DR SMR; Q3B1H8; -.
DR STRING; 319225.Plut_1961; -.
DR PRIDE; Q3B1H8; -.
DR EnsemblBacteria; ABB24803; ABB24803; Plut_1961.
DR KEGG; plt:Plut_1961; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002709; 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; Transcription; Transferase; Zinc.
FT CHAIN 1..1498
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000240814"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 69
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 82
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 499
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 867
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 950
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 953
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1498 AA; 166870 MW; F6AAA8C1419A7165 CRC64;
MIFSQGASPL KGDFTRIKFS IASPESILAH SRGEVLKPET INYRTFKPER DGLMCEKIFG
PTKDWECYCG KYKRVRYKGI ICDRCGVEVT TKSVRRERMG HISLAVPVVH TWFFRSVPSK
IGALLDLSTK ELERIIYYEV YVVINPGEPG EKQGIKKLDR LTEEQYFQII TEYEDNQDLE
DSDPQKFVAK MGGEAIHMLL KNLDLDGSAV LLRKILKESS SEQKRADALK RLKVVEAFRK
SYEPQRKVRK KSTGLFPEDD IPEPYIYEGN KPEYMVMEAI PVIPPELRPL VPLEGGRFAT
SDLNDLYRRV IIRNNRLKKL IDIRAPEVIL RNEKRMLQEA VDALFDNSRK ANAVKTGESN
RPLKSLSDAL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLHECGLPKS MAIELFQPFV
IRRLVERGIA KSVKSAKKLI DKKDPIVWDV LEKVIDGRPV LLNRAPTLHR LGIQAFQPTL
IEGKAIQIHP LVCTAFNADF DGDQMAVHVP LSQEAQLEAS LLMLSSHNLI LPQSGKPVTV
PSQDMVLGMY YLTKSRPGSL GEAGIFYSRE DVLIAHNEGR LGLHAQIFVQ YDGRLDQKFD
SLRALDWILE AGTEKYEWLK KQLEKKTMLL TTVGRVIFNE SVPEEIGFIN RVIDKKVAKE
LIGRLSSEVG NVETARFLDN IKQVGFHYAM KGGLSVGLSD AIVPETKAKH IKAAQRDSTR
VVKEYNRGTL TDNERYNQIV DVWQKTSNIV AEESYQKLKK DREGFNPLYM MLDSGARGSR
EQVRQLTGMR GLIARPQKSM SGQPGEIIEN PIISNLKEGL TVLEYFISTH GARKGLSDTS
LKTADAGYLT RRLHDVAQDV IVTMDDCGTT RGLFIQRNIE EETSGQIKFR EKIKGRVAAR
DIYDTITGNV IVPAGETITE ELAEIIQDTP GVEEAEIRSV LTCESKIGIC SRCYGTNLSV
HKLVEIGEAV GVIAAQSIGE PGTQLTLRTF HQGGTAQGGI SETETKAFNE GTVEFEDIKT
VYHAAINEDG VEEQHTIVIQ KNGKINIVDA ESGKVLKRYV VPHGAHLAVA PGDQVKKDQV
LFSSEPNSTQ IIAEINGTVK FADIEKGVTY KEEVDPQTGF AQHTIINWRS KLRATETREP
RLMIIDASGE VQKTYPVPIK SNLYVEDGQK VVPGDIMAKV PRNLDRVGGD ITAGLPKVTE
LFEARIPTDP AIVTEIDGYV SFGSQRRSSK EIKVKNDFGE EKVYYVQVGK HVLANEGDEV
KAGEPLTDGA VSPQDILRIQ GPNAVQQYLV NEIQKVYQIN AGVEINDKHL EVIVRQMLQK
VRVEEPGDTE LLPGDLIDRS VFLEANENVS EKVRISERGD APPRIQDDQL HRLREITKLN
RDLRKNEKQL IAFEPALQAT SHPVLLGITS AALQTESVIS AASFQETTKV LTDAAVAGKV
DHLAGLKENV IVGKLIPAGT GLKKYKAIRL GGEAIEASDA AAAAAEAEAQ ARREAMDE
