RPOC_BORBZ
ID RPOC_BORBZ Reviewed; 1377 AA.
AC B7J1W0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=BbuZS7_0390;
OS Borreliella burgdorferi (strain ZS7) (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=445985;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS7;
RX PubMed=20935092; DOI=10.1128/jb.01158-10;
RA Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA Mongodin E.F., Luft B.J.;
RT "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL J. Bacteriol. 193:1018-1020(2011).
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; CP001205; ACK74824.1; -; Genomic_DNA.
DR RefSeq; WP_012597363.1; NC_011728.1.
DR AlphaFoldDB; B7J1W0; -.
DR SMR; B7J1W0; -.
DR PRIDE; B7J1W0; -.
DR EnsemblBacteria; ACK74824; ACK74824; BbuZS7_0390.
DR KEGG; bbz:BbuZS7_0390; -.
DR HOGENOM; CLU_000524_3_1_12; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000006901; 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..1377
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141759"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 62
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 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 449
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 451
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 777
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 851
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 858
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 861
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1377 AA; 154637 MW; EAB53B852904E9E0 CRC64;
MKEIKDFERI KIKIASPDQI RNWSYGEVKK SETINYRTLR PEKDGLFCER IFGTTKEWEC
YCGKFKSVRY KGIICDRCNV EVTHFKVRRE RMGHIELAAP VAHIWYYKYI PSRIGLLLDI
TASSLNSILY YEKYVVIEPG DTDLKKMQLL NEDEYIEARE RYGMSFNASM GAEAIKTLLE
NLDLDELSSK LRIQMIDKDD KTDKKLLRRL EIIENFKISG NKPEWMIMEV LPVIPPEIRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLRK LLLLNAPEII VRNEKRMLQE SVDSLFDNSH
KRKVVKGSSS RPLKSLSDAL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLHQCGLPAK
MALELFKPFV IRRLIESEAV FNIKRAKNLI EQEVDEVWQI LDLVIKEHPI LLNRAPTLHR
LGIQAFEPVL VEGKAIKLHP LVCHAYNADF DGDQMAVHVP LTPAAQAESW ALMLSTNNLL
NPANGHPIVF PSQDIVLGLY YLTMEKKNVI GEGKKFLNFN NVILAINNRS LDYNASIYVK
IDGEYKKTTA GRVIFNEALP KGIEFVNKTL SDLELQILIS KVYVVHGSST VIEMLDIIKE
LGFRYATKFG CTISMSDIIV PDEKRTYVER ANKEIAKIQN DYAKGVITGE ERYNNVVSVW
LKTNEELTNK MMEILKKDRD GFNVIYMMAD SGARGSRNQI RQLAGMRGLM AKTSGDIIEL
PIISNFKEGL SVIEFFISTN GARKGLADTA LKTADAGYLT RRLVDIAQDV VVRIEDCGTI
NGIKVETVKN GEEILESLKE KAVGSYSIER IKNPITGEIV LDANEEISEA KIELLEKIGI
EKLVIRSVLT CEAEHGVCQK CYGRDFSKNK PVNIGEAVGI IAAQSIGQPG TQLTMRTFHI
GGVAQAGSED DKISLKNAFI LNGIEGFNVR VDNGILFTRK GTLKIINVFY EEKIKNIKEI
KVLDSQRVIK GIPLFIDKKG SEILSSYIGY VKLRDDNFFI VSEEQEVSLK AGTKLEIEVG
DYVESGKVIG TFDPFAEPII AEVKGKIKFK DIILGTTLKE EINTETGNVE KRITDNVFES
LDPRIFIIDS SGMEVASYVL PGDAYLQVED GQSINIGDII AKLSKGSEKT QDITGGLPRV
NDLFETRIPK NLTEMAKVSG IVQFKSIQKG KRLINILDEY GVEHKHYIPA GKHLLVRDGD
VVKAGDMLCD GRINPHDVLE ILGGISLQEF LLAEIQDVYR KQGVSINDKH IGVIIKQMMK
KVKIVAVGDT NFVYGQKVDK HTFYEQNRKV IKQGGEPAIA SPILIGVTKT SLNIDSFISA
ASFQETTKVL TDASIAGKID DLRGLKENVV IGHLIPTGTG MGLYKKIKVS ENIDSEV
