RPOC_CHLL2
ID RPOC_CHLL2 Reviewed; 1496 AA.
AC B3EER3;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Clim_0197;
OS Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290315;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 245 / NBRC 103803 / 6330;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Zhao F., Li T., Liu Z.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium limicola DSM 245.";
RL Submitted (MAY-2008) 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; CP001097; ACD89296.1; -; Genomic_DNA.
DR RefSeq; WP_012465177.1; NC_010803.1.
DR AlphaFoldDB; B3EER3; -.
DR SMR; B3EER3; -.
DR STRING; 290315.Clim_0197; -.
DR PRIDE; B3EER3; -.
DR EnsemblBacteria; ACD89296; ACD89296; Clim_0197.
DR KEGG; cli:Clim_0197; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008841; 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..1496
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353323"
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 1496 AA; 166732 MW; F6744FF6E3BDA487 CRC64;
MIFSQGASPL KGDFSRIKFS IASPESILAH SRGEVLKPET INYRTFKPER DGLMCEKIFG
PTKDWECYCG KYKRVRYKGI ICDRCGVEVT TKSVRRERMG HISLAVPVVH TWFFRSVPSK
IGALLDLSTK ELERIIYYEV YVVINPGEPG EKQGIKKLDR LTEEQYFQII TEYEDNQDLD
DTDSAKFVAK MGGEAIHMLL KSIDLNETAV TLRKVLRESS SEQKRADALK RLKVVESFRK
SYEPQKKTRK KPGGLFPEDE IPEPYVYEGN KPEYMVMEVV PVIPPELRPL VPLEGGRFAT
SDLNDLYRRV IIRNNRLKKL IDIRAPEVIL RNEKRMLQEA VDALFDNSRK ANAVKTGESN
RPLKSLSDAL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLHECGLPKS MAIELFQPFV
IRRLVERGIA KSVKSAKKLI DKKDPIVWDV LEKVIDGRPV LLNRAPTLHR LGIQAFQPVL
IEGKAIQIHP LVCTAFNADF DGDQMAVHVP LSQEAQLEAS LLMLSSHNLI LPQSGKPVTV
PSQDMVLGMY YLTKSRSGEE GEGRIFYDSE DVLIAYNEQR VGLHAQIFVC FNGLVDQKFD
PLRVLETVID EKSEKYGWLR SQLEQKKMLL TTVGRVIFNQ HVPESIGFIN RVIDKKVAKE
LIGRLSSEVG NVETAKFLDN IKEVGFHYAM KGGLSVGLSD AIVPETKVRH IKSAQKDSTK
VVKEYNRGTL TDNERYNQIV DVWQKTSNIV AEESYQKLKK DRDGFNPLYM MLDSGARGSR
EQVRQLTGMR GLIARPQKSM SGQPGEIIEN PIISNLKEGL TVLEYFISTH GARKGLSDTS
LKTADAGYLT RRLHDVAQDV IVTIDDCGTT RGLHVYRNIE EETSGQIKFR EKIRGRVAAR
DIYDTLNNNV VVKAGEIITD ELADLVQDTA GVEEAEIRSV LTCESKVGIC SKCYGTNLSV
HKLVEIGEAV GVIAAQSIGE PGTQLTLRTF HQGGTAQGGI SETETKAFNE GVLEFEDVKT
VEHSSINEDG VEDLRTIVIQ KNGKINIVDP ESGKVLKRYV IPHGAHLHCR PGNAVKKDQV
LFSSEPNSTQ IIAETPGSVR FADIEKGVTY KEEVDPQTGF AQHTIINWRS KLRANETREP
RIMIIDASGE IRKTYPVPIK SNLYVEDGQK VLPGDIIAKV PRNLDRVGGD ITAGLPKVTE
LFEARIPSDP AIVSEIDGYV SFGSQRRSSK EIKVKNDFGE EKIYYVQVGK HVLANEGDEV
KAGDPMTDGA VSPQDILRIQ GPNAVQQYLV NEIQKVYQIN AGVEINDKHL EVIVRQMLQK
VRVEEPGDTE LLPGDLIDRS AFIEANENIA EKVRVTDKGD APARIQDGQL CKMRDIAKLN
RELRKNSKKL VVIEPTLQAT SHPVLLGITS AALQTESVIS AASFQETTKV LTDAAVAGKI
DNLLGLKENV IVGKLIPAGT GLKRYRTIRL TGDTQKQAAV AEAVAAPDKE IEGHGI
