RPOC_BORRA
ID RPOC_BORRA Reviewed; 1377 AA.
AC B5RRJ6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=BRE_386;
OS Borrelia recurrentis (strain A1).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=412418;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1;
RX PubMed=18787695; DOI=10.1371/journal.pgen.1000185;
RA Lescot M., Audic S., Robert C., Nguyen T.T., Blanc G., Cutler S.J.,
RA Wincker P., Couloux A., Claverie J.-M., Raoult D., Drancourt M.;
RT "The genome of Borrelia recurrentis, the agent of deadly louse-borne
RT relapsing fever, is a degraded subset of tick-borne Borrelia duttonii.";
RL PLoS Genet. 4:E1000185-E1000185(2008).
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; CP000993; ACH94630.1; -; Genomic_DNA.
DR RefSeq; WP_012538866.1; NC_011244.1.
DR AlphaFoldDB; B5RRJ6; -.
DR SMR; B5RRJ6; -.
DR EnsemblBacteria; ACH94630; ACH94630; BRE_386.
DR KEGG; bre:BRE_386; -.
DR HOGENOM; CLU_000524_3_1_12; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000000612; 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_1000141763"
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; 154568 MW; 24246D5DFA28300B CRC64;
MKEIKDFEKI RIKIASPDQI RSWSYGEVKK SETINYRTLR PEKDGLFCER IFGTTKEWEC
YCGKFKSIRY KGIICDRCNV EVTHFKVRRE RMGHIELSAP VAHIWYYKYI PSRIGLLLDI
TASNLNSILY YEKYIVIEPG DTDLKKMQLL NEDEYSEAKE RYGMSFSASM GAEAIKTLLE
NLDLDELSSK LRLQMIDKDD KTDKKLLRRL EIIENFKISG NKPEWMIMDV LPVIPPEIRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLRK LLLLNAPEII VRNEKRMLQE SVDSLFDNSH
KRKVVKGTSN RPLKSLSDAL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLHQCGIPAK
MALELFKPFV IRKLIESEAV FNIKRAKSLI EQEVDEVWQI LDNVIKEHPV LLNRAPTLHR
LGIQAFEPVL VEGKAIKLHP LVCHAYNADF DGDQMAVHVP LTPAAQAESW ALMLSTNNLL
NPANGHPIVF PSQDIVLGLY YLTMERKNVM GEGRKFSNFN HVLLAINNKS LDYNAQIYVK
VGEEYIKTTA GRVVFSEALP GKISFVNKTL SDYELQTLIS EVYVIYGSSI VIEMLDIIKE
LGFRYATKFG CTISMSDIIV PQEKKVYVEK ANREIAKIQN DYTKGVITGE ERYNNVVSVW
SKTNEELTNK MMEILKKDRD GFNVIYMMAD SGARGSRNQI RQLAGMRGLM AKTSGDIIEL
PIISNFKEGL SVIEFFISTN GARKGLADTA LKTADAGYLT RRLVDIAQDV VVRIEDCGTI
NGIKVEALKN GEEIIEPLRE KAVGSYSIER IKSPITGEII LDVNEEITED KIKLLETVGI
DKLVIRSVLT CEAEHGVCQK CYGRDFSNNK PVSIGEAVGI IAAQSIGQPG TQLTMRTFHI
GGVAQAGSED DKIALKNAFI LNGLEGFNVQ VDGGLLFTRK GVLRIINVIY EESIKKIKKL
KVSDSQKVIK GMSLFIDKSG VEVLSSHIGY IKIKDNKLMI VSEEQEISLK VGTRLEINVG
DYVEAGRVIG TFDPFAEPII AEVKGKIKFK DIILGTTLKE EINLETGNIE KRITDQVFES
LDPRILIIND RGVEIASYVL PGDAYLQVED GQDIDIGDII AKLSKGSEKT QDITGGLPRV
NDLFETRIPK NLTEMAKVSG VVQFKAIQKG KRLINVIDEY GVEHKHYIPA GKHLLVRDGD
VVRAGDMLCD GRINPHDVLE ILGGISLQEF LLAEIQDVYR KQGVSINDKH IGVIIKQMMK
KVKIVSVGDT NFVYNQKVDK HAFYEQNKRV IEQGGEPAVA SPILIGITKA SLNIDSFISA
ASFQETTKVL TDASIAGSID DLRGLKENVV IGHLIPTGTG MNLYKRVKVR ENSNSEV
