RPOC_PELPB
ID RPOC_PELPB Reviewed; 1497 AA.
AC B4SG10;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=Ppha_2678;
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1;
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., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
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}.
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; CP001110; ACF44837.1; -; Genomic_DNA.
DR RefSeq; WP_012509309.1; NC_011060.1.
DR AlphaFoldDB; B4SG10; -.
DR SMR; B4SG10; -.
DR STRING; 324925.Ppha_2678; -.
DR PRIDE; B4SG10; -.
DR EnsemblBacteria; ACF44837; ACF44837; Ppha_2678.
DR KEGG; pph:Ppha_2678; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_10; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002724; 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; 1.
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..1497
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353402"
FT REGION 1476..1497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1497 AA; 167166 MW; F203721D50F8D9A2 CRC64;
MIFSQGASPL KGEFSRIKFS IASPESILAH SRGEVLKPET INYRTFKPER DGLMCEKIFG
PTKDWECYCG KYKRVRYKGI ICDRCGVEVT TKSVRRERMG HIALAVPVVH TWFFRSVPSK
IGALLDLSTK ELERIIYYEV YVVINPGEPG EKQGIKKLDR LTEEQYFQII TEYEDNQDLE
DSDPDKFVAK MGGEAIHMLL KNIDLDASAI HLRKVLKESN SEQKRADALK RLKVVEAFRK
SYEPHKKTRK KPQGLFPEDE LPEPYVYEGN KPEYMVMEVV PVIPPELRPL VPLEGGRFAT
SDLNDLYRRV IIRNNRLKKL IDIRAPEVIL RNEKRMLQEA VDALFDNSRK ANAVKTGESN
RPLKSLSDAL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLHECGLPKS MAIELFQPFV
IRRLVDRGIA KSVKSAKKLI DKKDPIVWDV LEKVIDGRPV LLNRAPTLHR LGIQAFQPLL
IEGKAIQIHP LVCTAFNADF DGDQMAVHIP LSQEAQLEAS LLMLSSHNLI LPQSGKPVTV
PSQDMVLGMY YLTKSRSRDL GEGQIFYSPQ DVLIAYNEER VGLHAQIFVQ YDGEIDQKFD
SLRVLDTMTD LTAEKSAWLK AQIEKKCILL TTVGRVIFNQ NVPKEIGFIN RVIDKKVAKE
LIGRLSSEVG NVETAKFLDN IKEVGFHYAM KGGLSVGLSD AIVPETKARH IKSAQRDSTK
VVKEYNRGTL TDNERYNQIV DVWQKTSNIV AEESYQKLKK DRDGFNPLYM MLDSGARGSR
EQVRQLTGMR GLIARPQKSM SGQPGEIIEN PIISNLKEGL TVLEYFISTH GARKGLSDTS
LKTADAGYLT RRLHDVAQDV IVTIDDCGTT RGLYVHRNIE EETSGQIKFR EKIKGRVAAR
DIIDTLNNNV IVNSGEIITE ELAELIQETA GVEEAEIRSV LTCESKIGIC SKCYGTNLSV
HELVEIGEAV GVIAAQSIGE PGTQLTLRTF HQGGTAQGGI SETETKAFYD GQIQFEDIKT
VEHTAINEDG VADLRIIVIQ KNGKINIADP ESGKILKRYL VPHGAHLHCK NGSLVKKDQV
MFSSEPNSTQ IIAEIPGIIK FADIEKGITY KEEVDPQTGF SQHTIINWRS KLRATETREP
RLMIIDASGE VRKTYPVPIK SNLYVEDGQK VEPGDIMAKV PRNLDRVGGD ITAGLPKVTE
LFEARIPTDP AIVTEIDGYV SFGSQRRSSK EIKVKNDFGE EKVYYVQVGK HVLANEGDEV
KAGDPLTDGA VSPQDILRIQ GPNAVQQYLV NEIQKVYQIN AGVEINDKHL EVIVRQMLQK
VRVEEPGDTD LLPGDLIDRS AFVESNQSVA EKVRITEKGD APARIQDSQL HKVRDITKLN
RELRKNSKNM IAFEPALQAT SHPVLLGITS AALQTESVIS AASFQETTKV LTDAAVAGKV
DYLAGLKENV IVGKLIPAGT GLKRYKAIKL TGEGQESNAT ERVVEEPATR EGFANER
