RPOC_POLAQ
ID RPOC_POLAQ Reviewed; 1420 AA.
AC A4SUV5;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Pnuc_0047;
OS Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Polynucleobacter.
OX NCBI_TaxID=312153;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX PubMed=22675600; DOI=10.4056/sigs.2395367;
RA Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT "Complete genome sequence of Polynucleobacter necessarius subsp.
RT asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP33269.1; -; Genomic_DNA.
DR RefSeq; WP_011901895.1; NC_009379.1.
DR AlphaFoldDB; A4SUV5; -.
DR SMR; A4SUV5; -.
DR STRING; 312153.Pnuc_0047; -.
DR PRIDE; A4SUV5; -.
DR EnsemblBacteria; ABP33269; ABP33269; Pnuc_0047.
DR GeneID; 31480393; -.
DR KEGG; pnu:Pnuc_0047; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_4; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000231; 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..1420
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353406"
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 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 823
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"
FT BINDING 904
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 907
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1420 AA; 156199 MW; 93C5AD26ACDCE885 CRC64;
MKALLDLFKQ TQGDEQFDVI KIGLASPEKI RSWSFGEVRK PETINYRTFK PERDGLFCAK
IFGPTKDYEC LCGKYKRLKF RGVICEKCGV EVTLAKVRRE RMGHIELAAP VAHIWFLKSL
PSRLGMVLDM TLRDIERVLY FEAYVVVDPG MTPEGAMKRG QIMSEDEYIA KTEEYGDGAF
TAIMGAEGIR DLLRGIDIDR EVETIRADLK ATGSDAKIKK YAKRLKVLEA FQTSGIKPDW
MIMEVLPVLP PELRPLVPLD GGRFATSDLN DLYRRVINRN NRLKRLLELR APEIIVRNEK
RMLQEAVDSL LDNGRRGKAM TGANKRPLKS LAEMIKGKSG RFRQNLLGKR VDYSGRSVIV
VGPTLKLHQC GLPKLMALEL FKPFIFNKLE TLGIATTIKA AKKEVESQTP IVWDILEEVI
REHPIMLNRA PTLHRLGIQA FEPMLIEGKA IQLHPLVCAA FNADFDGDQM AVHVPLSLEA
QMEARTLMLA SNNVLFPANG EPSIVPSQDV VLGLYYATRD KINGKGEGMV FANIAEVIRA
HEAGQVELAS RVAVRITEFE IVDKKAEGDA RFAEKTKIYQ TSVGRAILSE ILPKGMTFEE
INKPLKKKEI SRLINTSFRK CGLRETVIFA DRLLQSGFRL ATNAGISVAI DDMLIPTSKE
RIITEATNKV KEYDKQFMSG LVTNQERYNN VVDIWGAAGD QVGKAMMDEL SHVDVLDRNS
KTVRQESFNS IYMMADSGAR GSAAQIRQLA GMRGLMAKPD GSIIETPITA NFREGLNVLQ
YFISTHGARK GLADTALKTA NSGYLTRRLC DVTQDLVVIE DDCGATSGVT MKALVEGGEI
IEALRDRILG RVCIGDIVHP DTQEVIVAND TLLDEDHVDQ IVALGIDEVK VRTVLSCLTR
FGLCAKCYGR DLGRGGLVNV GEAVGVIAAQ SIGEPGTQLT MRTFHIGGAA SRALVASNIE
AKSNGALKFS GTMRIVKNAK GEQIVISRSG EALIIDDNGR ERERHKVPYG ATLLFKEDAA
VKAGASLATW DPLTRPIISE YAGIARFDNV EEGVTVAKQV DEVTGLSTLV VIDGKRRSAA
SKGVRPMINL VDDKGGEVMI AGTDHPVNIG LQVGALITVK DGQKVEVGEV LARIPIESQK
TRDITGGLPR VAELFEARSP KDAAVLAKVT GTVSFGKETK GKQRLVITDM DGEANEFLIP
KEKQVLVHDG QVVNKGEMIV EGPADPHDIL TLRGIEELAI YIVDEVQDVY RLQGVKINDK
HIEVIVRQML RRVQITDGGD TAYITGEQVE RSKLYDANDL VIAAGKRPAQ FENVLLGITK
ASLSTDSFIS AASFQETTRV LTEAAIMGKT DTLRGLKENV IIGRLIPAGT GLSYRRARKV
REQFERDRAQ MIAAEEEAIA NTPVEIEAEV IAPAGEADPS
