RPOC_PROA2
ID RPOC_PROA2 Reviewed; 1499 AA.
AC B4S498;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-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=Paes_0289;
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413;
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., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
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; CP001108; ACF45346.1; -; Genomic_DNA.
DR RefSeq; WP_012504883.1; NC_011059.1.
DR AlphaFoldDB; B4S498; -.
DR SMR; B4S498; -.
DR STRING; 290512.Paes_0289; -.
DR EnsemblBacteria; ACF45346; ACF45346; Paes_0289.
DR KEGG; paa:Paes_0289; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002725; 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..1499
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353407"
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 1499 AA; 166785 MW; 1ED32BD326A25EDA CRC64;
MIFSQGSSPF KGDFSKIKFS IASPESVLAH SRGEVLKPET INYRTFKPER DGLMCEKIFG
PTKDWECYCG KYKRVRYKGI ICDRCGVEVT MKSVRRERMG HISLAVPVVH TWFFRSVPSK
IGALLDLSTK ELERIIYYEV YVVINPGDPG EKQGIKKLDR LTEEQYFQII TEYEDNQDLD
DDDPAKFVAK MGGEAIHTLL KGLNLDESAV GLRKVLKESG SEQKRADALK RLKVVEAFRK
SYEPQKKTRK KPGGLFPEDE MPEPYIFEGN KPEYMVMEVI 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 YLTKSRIGEN GQGNIFYSNE EVLIAHNEER LGLHALVFIK YDGHVEQKFD
PVRLLDIISD DESEKKAWLK KEIEAKRLLV TTVGRVIFNQ YVPEKIGFVN KVIDKKGAKE
LISKICSEVG NVQAAEFLDN IKQVGYHYAM KGGLSIGLAD AIIPEAKIQL IKKATKESNK
ILREYNRGTL TENERYNQIV DVWQKVTNLV AEESYQKLRK DRVGFNPLFM MLDSGARGSR
EQVRQLTGMR GLIARPQKSM SGQPGEIIEN PIISNLKEGL TVLEYFVSTH GARKGLSDTS
LKTADAGYLT RRLHDVAQDV IVTIDDCGTT RGLHVERSIE EETGGQIKFS DKIRGRVASR
DIWDTLKDEI VVPAGGIITE DIADAIQANI GVLEADIRSV LTCEAKQGIC SKCYGTNLAV
HKIVEIGEAV GVIAAQSIGE PGTQLTLRTF HQGGTAQGGI AETETKAVYE GQVEFENIRT
VEQETINEDG MPEVRILVIQ KNGRINIVDP DSGKVLKRHD VPHGASLHRS VGDLVKKEDV
LFSSEPNSTQ IIAELEGYVK FADIEKGVTY KEEVDPQTGY VQHVIINWRS KLRASETREP
RIMIVSESGE ILKTYPVPIK SNLFVEDNKK VSIGDILAKV PRNLDRVGGD ITAGLPKVTE
LFEARIPSDP AIVSEIDGYV GFGSQRRSSK EIKVKNEFGE EKTYYVQVGK HVLANEGDEV
TAGEPLTDGA ISPQDILRIQ GPNAVQQYLV NEIQKVYQIN AGVEISDKHL EVIVRQMLQK
VRVEEPGDTE LLPGDLIDRT VFIEANTAIA EKVRVIDKGD APARIQEDQL YKLKEITKLN
RELRKNSKSL IVVEPAIQAT SHPVLLGITS AALQTESVIS AASFQETTKV LTDAAVAGKI
DNLLGLKENV IVGKLIPAGT GLKAYRKLEL NKVYPEAAEI AVPEVDEAAP ASSDDDAAE
