RPOC_PELUB
ID RPOC_PELUB Reviewed; 1389 AA.
AC Q4FLL3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=SAR11_1122;
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; Candidatus Pelagibacter.
OX NCBI_TaxID=335992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062;
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(2005).
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; CP000084; AAZ21925.1; -; Genomic_DNA.
DR RefSeq; WP_011282158.1; NC_007205.1.
DR AlphaFoldDB; Q4FLL3; -.
DR SMR; Q4FLL3; -.
DR STRING; 335992.SAR11_1122; -.
DR PRIDE; Q4FLL3; -.
DR EnsemblBacteria; AAZ21925; AAZ21925; SAR11_1122.
DR GeneID; 66295611; -.
DR KEGG; pub:SAR11_1122; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_5; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002528; 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; -; 2.
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..1389
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225560"
FT BINDING 73
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 468
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 810
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1389 AA; 154508 MW; 44E6EE1CFCC4E577 CRC64;
MKKELTDLFK NSEVSEAQNF NSIKITLASP EKIKSWTYGE IKKPETINYR TFRPEKDGLF
CARIFGPIKD YECLCGKYKR MKFRGIICEK CGVEVTKSNV RRERMGHINL ATPVAHIWFL
KSLPSRISLA VDMKLKEVER VLYFENFIVI EPGLTGLQKN QLLNEEELAK YQDEFGEESF
EAGIGAEAIL SILKSMDLEL ERKLLINTIK ETKSKVNEER SIKRLKLIES FIETGQKPEW
MILTVIPVIP PELRPLVPLD GGRFATSDLN DLYRRVINRN NRLKRLMDLK APDIIVRNEK
RMLQESVDAL FDNGRRGRVI TGTGKRPLKS LAEMLKGKQG RFRQNLLGKR VDYSGRSVIV
VGPDLKLHEC GLPKKMALEL FKPFLYARLN KLGLASTIKQ AKKLVEKETN AVWDALELIV
REHPVLLNRA PTLHRLGVQA FEPKLIEGDA IELHPLCCAA FNADFDGDQM AVHVPLSLEA
QLEARILMLS TNNILSPSNG KPIIVPSQDM ILGLYYLSQA PFQTEKPDGY FINNDEIEHA
LSTGQIKVHS TIVSRFETLD EKGNKRVEKH TTTAGRFLLA NLLPKHKDIT FSMIDRLLPK
KTVSEIIDSV FRFCGQKTTV IFCDHLKDLG FKHAFKAGIS FGKDDLVIPA NKGQLIEDTK
KLIADYENQY SEGLITRGEK YNKVVDAWSK CTDKVAGEMM RGISATESTP DGMKINSVFM
MADSGARGSA AQMKQLAGMR GLIAKPSGEI IETPIISNFK EGLTALEYFN STHGARKGLA
DTALKTASSG YLTRRLCDVA QDLTISKIKC DNPGFIELAE ILEGGNVVVS LSERALGRVT
AFDVKNPITG EVVIKKETMI DEAGCDKIDA AGVKFIKAYS VMTCSSKLGV CATCYGRDLS
RGKMVHVGEA IGMISAQSIG EPGTQLTMRT FHVGGTASVK QESQIVTKTA GTLKIINSNL
LEDSKKNLIV MGRNTQLSIE DNNGVQVAVY KVAYGSKLFF QNGDKVKANE KICEWDPYTT
PVIAEKSGIA GYVDLIDGVS IQETTDDATG ISSKSVIDWR AQSKNTDLKP RITLRDDKGN
VIKKADDNEA RYYLVPDSIL SVKDGQKIFA GDIIARLPKE TTKTKDITGG LPRVAELFEA
RKAKDSAIIA ENDGQVLFGK EVRGKQRISI QPDNGEPSNY LIPKGKHINF NQGEKIKKGE
YLLDGQPLPH DILRILGIKD LTEYFVNQVQ EVYRLQGVII NDKHIETILR QMLKKVEIKE
SGDSSYLPGE MIDRIKFDNT NEKLVAEGKN PASGERVLMG ITKASLQTES FISAASFQET
TRVLTDAAIK GKVDPLNGLK ENVIVGRLVP AGTGHIKNKW NKNAIDADNK FLAEQEKIEP
LETTETPAN
