RPOC_CHLP8
ID RPOC_CHLP8 Reviewed; 1494 AA.
AC B3QQS1;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=Cpar_1882;
OS Chlorobaculum parvum (strain DSM 263 / NCIMB 8327) (Chlorobium vibrioforme
OS subsp. thiosulfatophilum).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae; Chlorobaculum.
OX NCBI_TaxID=517417;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 263 / NCIMB 8327;
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., Mikhailova N., Zhao F., Li T., Liu Z., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobaculum parvum NCIB 8327.";
RL Submitted (JUN-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; CP001099; ACF12274.1; -; Genomic_DNA.
DR RefSeq; WP_012503107.1; NC_011027.1.
DR AlphaFoldDB; B3QQS1; -.
DR SMR; B3QQS1; -.
DR STRING; 517417.Cpar_1882; -.
DR PRIDE; B3QQS1; -.
DR EnsemblBacteria; ACF12274; ACF12274; Cpar_1882.
DR KEGG; cpc:Cpar_1882; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008811; 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..1494
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353322"
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 868
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 944
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 951
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 954
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1494 AA; 166471 MW; 604926CCF229EC85 CRC64;
MIFSQGSSPI KGDFSKIKFS IASPESILAH SRGEVLKPET INYRTFKPER DGLMCEKIFG
PTKDWECYCG KYKRVRYKGI ICDRCGVEVT TKNVRRERMG HISLAVPVVH TWFFRSVPSK
IGALLDLSTK ELERIIYYEV YVVINPGEPG EKQGIKKFDR LTEEQYFQII TEYEDNQDLE
DNDPAKFVAK MGGEAIHTLL KGLNLDEIAV NLRKVLKESG SEQKRADALK RLKVVESFRK
SYEPQKRTRK KSTGLFPEED SPELYIYEGN KPEYMVMEVV PVIPPELRPL VPLEGGRFAT
SDLNDLYRRV IIRNNRLKKL IDIRAPEVIL RNEKRMLQEA VDALFDNSRK ANAVKTGESN
RPLKSLSDAL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL QLHQCGLPKS MAIELFQPFV
IRRLVERGIA KSVKSAKKLI DKKDPVVWDV LEKVIDGRPV LLNRAPTLHR LGIQAFQPTL
IEGKAIQLHP LVCTAFNADF DGDQMAVHVP LSQEAQLEAS LLMLSSHNLI LPQSGKPVTV
PSQDMVLGMY YLTKARFGDV GQGQLFYSME EVIIAYNEER AGLHAQIFVK YDGKVDQVSD
PVRLVDTLVP EEQAERRAWL KSQIEQKKVL VTTVGRVIFN QHMPEKIGFI NKLINKKVAK
ELIAHLSSQV GNVETAQFLD NIKAVGFGYA MRGGLSIGLS DAIVPETKVK HIKNAQRDSA
KVVKEYNRGT LTDNERYNQI VDVWQKTSNL VADESYQKLK NDRDGFNPLY MMLDSGARGS
REQVRQLTGM RGLIARPQKS MSGQPGEIIE NPIISNLKEG LTVLEYFIST HGARKGLSDT
SLKTADAGYL TRRLHDVAQD VIVTIDDCGT TRGLHVERNI EEETSGQIKF REKIKGRVAA
RDIVDVINDK VVVKAGEIIT DELAAAIQDN IGVEEAEIRS VLTCESKVGI CSKCYGTNLS
VHKLVEMGEA VGVIAAQSIG EPGTQLTLRT FHQGGAAQGG ISETETKAFY EGQVELEDVK
SVEHSIITED GIEETRQIVI QKNGKLNIID PDSGKVLKRY VVPHGAHINV ENGQMVRKDQ
VLFSSEPNST QILAEMPGFA KFIDIEKGVT YKEEVDPQTG FAQHTIINWR SKLRASETRE
PRIAIVSESG EIKKTYPVPI KSNLYVEDGQ KLNPGDTIAK VPRNLDRVGG DITAGLPKVT
ELFEARIPTD PAIVSEIDGY VSFGSQRRSS KEIKVKNDFG EEKTYYVQVG KHVLATEGDE
VKAGDPLTDG AVSPQDILRI QGPNAVQQYL VNEIQKVYQI NAGVEINDKH LEVIVRQMLQ
KVRVEEAGDT NLLPGDLIDR GTFIEANEAV AEKVRVIDRG DAPPRIQEGQ LYKQRDITKL
NRELRRNSKS LITIEPALQA TSHPVLLGIT SAALQTESVI SAASFQETTK VLTDAAVAGK
VDHLAGLKEN VIVGKLIPAG TGLRKYRSIR LQSNEPEEVD VIESASTGDA EEEN
