RPOC_ELUMP
ID RPOC_ELUMP Reviewed; 1385 AA.
AC B2KEN0;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Emin_1427;
OS Elusimicrobium minutum (strain Pei191).
OC Bacteria; Elusimicrobia; Elusimicrobia; Elusimicrobiales;
OC Elusimicrobiaceae; Elusimicrobium.
OX NCBI_TaxID=445932;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pei191;
RX PubMed=19270133; DOI=10.1128/aem.02698-08;
RA Herlemann D.P.R., Geissinger O., Ikeda-Ohtsubo W., Kunin V., Sun H.,
RA Lapidus A., Hugenholtz P., Brune A.;
RT "Genomic analysis of 'Elusimicrobium minutum,' the first cultivated
RT representative of the phylum 'Elusimicrobia' (formerly termite group 1).";
RL Appl. Environ. Microbiol. 75:2841-2849(2009).
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; CP001055; ACC98976.1; -; Genomic_DNA.
DR RefSeq; WP_012415591.1; NC_010644.1.
DR AlphaFoldDB; B2KEN0; -.
DR SMR; B2KEN0; -.
DR STRING; 445932.Emin_1427; -.
DR PRIDE; B2KEN0; -.
DR EnsemblBacteria; ACC98976; ACC98976; Emin_1427.
DR KEGG; emi:Emin_1427; -.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001029; 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..1385
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353350"
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 74
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 467
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 829
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 910
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 917
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 920
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1385 AA; 152805 MW; 39274280B790C358 CRC64;
MSEKTKKTKR LDDLNFFDFD AIKLGIASPE QIMAWSHGEV KKPETINYRT LKPERDGLFC
ERIFGPTKDY ECSCGKYRWV KYKGMQCDRC GVEITEAKVR RERMGHLELA VPVAHVWFLR
KNPSRIGIML DMRITDLERV VYYASYVVVE DCIDSVTGRT DYKKGELLTD VQVREARKKH
GSRLKVDIGA PAVKKLLSDI DFDKEIPTLH VQLAETQSEL ERTKLIRRIK TMEEFKASGN
RPEWMILSVL PVIPPDLRPL VPLDGGRFAA SDLNDLYRRI INRNNRLKHI ESLRAPEVMI
YNEKRLLQEA VDALIENGAR GKFFIGAGGR PLKSLSDVIK GKHGRFRQNL LGKRVDYSGR
SVIVVGPSLK LHQCGLPKLM ALELFKPFII GELMKKEGVT LKAAKKMLER VRPEIWDILE
QVTKNHPVML NRAPTLHRLG IQAFEPVLIE GKAIQLHPLT CAAFNADFDG DQMAVHVPLS
LEAQLEARTL MLATNNILSP ASGRPIAAPS HDIVMGISFL TKVKLNDFGE GAVFGSMEEA
LMAYAYGKVS LHARIKVRGI TAIKEDGMNE KDLKNVNTWK DYTTVGKIIF NNNLPEGWPY
VNGAVGKKEL AAIIDECYKS KKYGKYETVQ LLDRIMKLGY NYATRSGLSI SIADMIVPAA
KQKYIDAAKK RIKEIQGQAE AGIITEGERY NKVIDIWTRV TDDVAVEQFK EMKKFEEAPY
SGEGQRFNSV FLMADSGARG SRQQVRQLAG MRGLMAKPQK KLTGGQGEII ESPITSNFRE
GLSVLEYFIS THGGRKGLSD TALKTAEAGY LTRRLIDVAH NLVVMEEDCG TTNGVVVSSL
MSGEEVVEPI EERILGRTSL EDVIVKIKKA DGKEEEKTII KEGDSITLEQ SKLVKKYGVQ
NLRIRSVLTC ESKNGVCGKC YGVSLVSGNI SNVGDSVGII AAQSIGEPGT QLTLRTFHIG
GAASRMLSQS QAVAELGGKV TFKDIKVITN RFDNKICISR NGAIFVEAAN GTIKEYKIQY
GATLHIADKV TVEKGTLMAE WDPHSIPVLS ETEGTARLTD VSEGITLQEE RNKVTGVIER
KITASRMGKK NPRIVIEGKG GKKVSLPLPV DTILLVENGE DVLAGDILAK IAKASGGTKD
ITSGLPRIAE LFEARKPRNA AIMSEFAGVV SLETSPKGLV EIVVRSEETG QVKQYAVPQG
KHLVVYEGDH VGVGEALTDG AIDPHDVLRV KGIKEVQEFL LNAIQEVYRL QGVTINDRHI
EVIVRQMLGN VKIVDAGDTP LLKGEIVSRA TLLKHNAQAE KEGKKIAVGD PILLGISKAS
LASDSFISAA SFQETTKVLT DAAITGQVDT LQGLKENVIV GHLIPAGTGI SAREFTKEFE
AAKKK
