RPOC_METPP
ID RPOC_METPP Reviewed; 1412 AA.
AC A2SLG4;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=Mpe_A3450;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(2007).
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; CP000555; ABM96403.1; -; Genomic_DNA.
DR RefSeq; WP_011831024.1; NC_008825.1.
DR AlphaFoldDB; A2SLG4; -.
DR SMR; A2SLG4; -.
DR STRING; 420662.Mpe_A3450; -.
DR PRIDE; A2SLG4; -.
DR EnsemblBacteria; ABM96403; ABM96403; Mpe_A3450.
DR KEGG; mpt:Mpe_A3450; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000366; 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..1412
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308852"
FT REGION 1388..1412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
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 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 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 813
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 887
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"
FT BINDING 897
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1412 AA; 155396 MW; EB9C885F58ACE551 CRC64;
MKGLLDLFKQ FTPDEHFDAI KIGLASPEKI RSWSFGEVKK PETINYRTFK PERDGLFCAK
IFGPIKDYEC LCGKYKRLKH RGVICEKCGV EVTQTKVRRD RMGHIDLAAP CAHIWFLKSL
PSRLGLVLDM TLRDIERVLY FEAYVVVDPG MTELKKFSIM TEDDYDAKKQ QHGDEFVALM
GAEGIQKLLA EIDLDVEIER LRGDMTGSEL KVKKNSRRLK VMEAFKKSGI KPQWMVMNVL
PVLPPDLRPL VPLDGGRFAT SDLNDLYRRV INRNNRLARL LELKAPEIIV RNEKRMLQEA
VDSLLDNGRR GKAMTGANKR ALKSLADMIK GKSGRFRQNL LGKRVDYSGR SVIVVGPTLK
LHQCGLPKLM ALELFKPFIF SRLEAMGIAT TIKAAKKEVE SGTPVVWDIL EEVIKEHPVM
LNRAPTLHRL GIQAFEPVLI EGKAIQLHPL VCAAFNADFD GDQMAVHVPL SIEAQMEART
LMLASNNVLF PANGEPSIVP SQDVVLGLYY ATRDRINAKG EGLIFSDVVE VQRALDNGQV
EITAKIAVRL TEWTKDKESG EFVPESKLVD TTVGRALLSE ILPKGLPFAN INKALKKKEI
SRLINTSFRK CGLKETVVLA DKLLQSGFRL ATRAGISISI DDMLVPKQKH DLIERAEKEV
KEIEQQYVSG LVTAGERYNK VVDIWGKTGD EVGKVMMAQL SKQKVEDRHG KLVDQESFNS
IYMMADSGAR GSAAQIRQLA GMRGLMAKPD GSIIETPITA NFREGLNVLQ YFISTHGARK
GLADTALKTA NSGYLTRRLV DVTQDLVVTE DDCGTDAGIA MRALVEGGEV IESLRDRILG
RVTAIEVLHP ETQQVVVPAG LMLDEDTLDI VEAAAVDEVK VRTPLTCHTR FGLCAKCYGR
DLGRGGLVNA GEAVGVIAAQ SIGEPGTQLT MRTFHIGGAA SRAAVASSVE AKSDGHIGFN
ATMRYVTNGK GELVVISRSG EIIISDQHGR ERERHKVPYG ATLNIKADQQ VKAGTVLANW
DPLTRPIITE FAGKAKFENV EEGVTVAKQV DEVTGLSTLV VIDPKRRGAA KVVRPQVKLL
DAAGNEVKIP GTDHSVTIGF PIGSLVQIRD GQDLAPGEVL ARIPVEGQKT RDITGGLPRV
AELFEARTPK DKGTLAEMTG TVSFGKETKG KVRLQITDPD GKVYEELVPK EKNILVHEGQ
VVNKGESIVD GPADPQDILR LLGIEELARY IVDEVQDVYR LQGVKINDKH IEVIVRQMLR
RVQIVNPGDT HYILGEQVER ASMLDTNDKM RAEGKMIATH ADVLLGITKA SLSTDSFISA
ASFQETTRVL TEAAIMGKRD ELRGLKENVI VGRLIPAGTG LAFHRARKAK EEMDDAERRS
IALQEAEEQA LLTPATTAEA VVGEEPAPPP AQ
