RPOC_BORAP
ID RPOC_BORAP Reviewed; 1377 AA.
AC Q0SNB9; G0IS35;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
GN OrderedLocusNames=BAPKO_0403, BafPKo_0390;
OS Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=390236;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=16914037; DOI=10.1186/1471-2164-7-211;
RA Gloeckner G., Schulte-Spechtel U., Schilhabel M., Felder M., Suehnel J.,
RA Wilske B., Platzer M.;
RT "Comparative genome analysis: selection pressure on the Borrelia vls
RT cassettes is essential for infectivity.";
RL BMC Genomics 7:211-211(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PKo;
RX PubMed=22123755; DOI=10.1128/jb.05951-11;
RA Casjens S.R., Mongodin E.F., Qiu W.G., Dunn J.J., Luft B.J.,
RA Fraser-Liggett C.M., Schutzer S.E.;
RT "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT Lyme disease agent isolates.";
RL J. Bacteriol. 193:6995-6996(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}.
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DR EMBL; CP000395; ABH01659.1; -; Genomic_DNA.
DR EMBL; CP002933; AEL69616.1; -; Genomic_DNA.
DR RefSeq; WP_004790677.1; NC_017238.1.
DR AlphaFoldDB; Q0SNB9; -.
DR SMR; Q0SNB9; -.
DR STRING; 390236.BafPKo_0390; -.
DR EnsemblBacteria; AEL69616; AEL69616; BafPKo_0390.
DR KEGG; baf:BAPKO_0403; -.
DR KEGG; bafz:BafPKo_0390; -.
DR PATRIC; fig|390236.22.peg.383; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_12; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000005216; 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_0000308822"
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; 154472 MW; A82E37D9E77F3F8B CRC64;
MKEIKDFEKI KIKIASPDQI RNWSYGEVKK SETINYRTLR PEKDGLFCER IFGTTKEWEC
YCGKFKSVRY KGIICDRCNV EVTHFKVRRE RMGHIELAAP VAHIWYYKYI PSRIGLLLDI
TASSLNSILY YEKYVVIEPG DTDLKKMQLL NEDEYIEARE RYGMSFNASM GAEAIKSLLE
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 LTPSAQAESW ALMLSTNNLL
NPANGHPIVF PSQDIVLGLY YLTMEKKNTV GEGKKFLNFN NVILAINNRS LDYNASIYVK
IDGKYKKTTA GRVIFNEALP NGIEFVNKTL SDLELQILIS KVYVVHGSST VIEMLDIIKE
LGFKYATKFG CTISMSDIIV PDEKKAYIDR 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 DKISLKNTFI LNGIEGFNVR VENGILFTRK GTLKIINVFY EEKIKNIKEI
KVSDSQRVIK GIPLFVNNKG VEILSSYIGY VKLRDDKFLI VSEEQEVSLK AGTKLEIEVG
EYVESGKVIG TFDPFAEPII AEVKGKIKFK DIILGTTLKE EINTETGNVE KRITDNVFES
LDPRIFIIDS GGVEIASYVL PGDAYLQVED GQNINIGDII AKLSKGSEKT QDITGGLPRV
NDLFETRIPK NLTEMAKVSG IVQFKSIQKG KRLINILDEY GVEHKHYIPA GKHLLVRDGD
IVKAGDMLCD GRINPHDVLE ILGGISLQEF LLAEIQDVYR KQGVSINDKH IGVIIKQMMK
KVKIVAVGDT NFVYGQKVDK HTFYEQNRKV IEQGGEPAIA SPILIGVTKT SLNIDSFISA
ASFQETTKVL TDASIAGKID DLRGLKENVV IGHLIPTGTG MGLYKKIKVS ENVNSEV
