ID RPOC_BORBU Reviewed; 1377 AA.
AC O51349; Q45035;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 27-MAR-2024, entry version 138.
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=BB_0388;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9074501; DOI=10.1016/s0378-1119(96)00714-7;
RA Alekshun M., Kashlev M., Schwartz I.;
RT "Molecular cloning and characterization of Borrelia burgdorferi rpoB.";
RL Gene 186:227-235(1997).
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; AE000783; AAB91502.1; -; Genomic_DNA.
DR EMBL; L48488; AAC37119.1; -; Genomic_DNA.
DR PIR; C70148; C70148.
DR RefSeq; NP_212522.1; NC_001318.1.
DR RefSeq; WP_010889741.1; NC_001318.1.
DR AlphaFoldDB; O51349; -.
DR SMR; O51349; -.
DR STRING; 224326.BB_0388; -.
DR PaxDb; 224326-BB_0388; -.
DR EnsemblBacteria; AAB91502; AAB91502; BB_0388.
DR KEGG; bbu:BB_0388; -.
DR PATRIC; fig|224326.49.peg.783; -.
DR HOGENOM; CLU_000524_3_1_12; -.
DR OrthoDB; 9815296at2; -.
DR Proteomes; UP000001807; 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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd02655; RNAP_beta'_C; 1.
DR CDD; cd01609; RNAP_beta'_N; 1.
DR Gene3D; 1.10.132.30; -; 1.
DR Gene3D; 1.10.150.390; -; 1.
DR Gene3D; 1.10.1790.20; -; 1.
DR Gene3D; 1.10.40.90; -; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 4.10.860.120; RNA polymerase II, clamp domain; 1.
DR Gene3D; 1.10.274.100; RNA polymerase Rpb1, domain 3; 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 NCBIfam; TIGR02386; rpoC_TIGR; 1.
DR PANTHER; PTHR19376; DNA-DIRECTED RNA POLYMERASE; 1.
DR PANTHER; PTHR19376:SF54; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 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..1377
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067711"
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"
FT CONFLICT 17
FT /note="P -> S (in Ref. 2; AAC37119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1377 AA; 154658 MW; 160DD492579ED4D0 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 YLTMEKKNVV GEGKKFLNFN NVILAINNRS LDYNASIYVK
IHGEYKKTTA GRVIFNEALP KGIEFVNKTL SDLELQILIS KVYVVHGSSI 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 IEQGGEPAIA SPILIGVTKT SLNIDSFISA
ASFQETTKVL TDASIAGKID DLRGLKENVV IGHLIPTGTG MGLYKKIKVS ENIDSEV
//
