RPOC_BORT9
ID RPOC_BORT9 Reviewed; 1377 AA.
AC A1QZH6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=BT0388;
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borrelia.
OX NCBI_TaxID=314724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135;
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
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; CP000049; AAX17718.1; -; Genomic_DNA.
DR RefSeq; WP_011772337.1; NC_008710.1.
DR AlphaFoldDB; A1QZH6; -.
DR SMR; A1QZH6; -.
DR STRING; 314724.BT0388; -.
DR PRIDE; A1QZH6; -.
DR KEGG; btu:BT0388; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_12; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001205; 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; -; 2.
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_1000165835"
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; 154543 MW; 95697E0CD8820F0A CRC64;
MKEIKDFEKI RIKIASPDQI RSWSYGEVKK SETINYRTLR PEKDGLFCER IFGTTKEWEC
YCGKFKSIRY KGIICDRCNV EVTHFKVRRE RMGHIELSAP VAHIWYYKYI PSRIGLLLDI
TASNLNSILY YEKYIVIEPG DTDLKKMQLL NEDEYSEAKE RYGMSFSASM GAEAIKTLLE
NLDLDELSSK LRLQMIDKDD KTDKKLLRRL EIIENFKVSG NKPEWMIMDV LPVIPPEIRP
MVQLDGGRFA TSDLNDLYRR VINRNNRLRK LLLLNAPEII VRNEKRMLQE SVDSLFDNSH
KRKVVKGTSN RPLKSLSDAL KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KLHQCGIPAK
MALELFKPFV IRKLIESESV FNIKRAKSLI EQEVDEVWQI LDNVIKEHPV LLNRAPTLHR
LGIQAFEPVL VEGKAIKLHP LVCHAYNADF DGDQMAVHVP LTPAAQAESW ALMLSTNNLL
NPANGHPIVF PSQDIVLGLY YLTMERKNVV GEGRKFSNFN HVLLAINNKS LDYNARIYVK
VDGEYIETTA GCVVFNEALP GKISFVNKTL SDYELQNLIS EVYVVYGSSI VIEMLDIIKE
LGFKYATKFG CTISMSDIIV PEEKKVYVDK ANREIAKIQN DYTKGVITGE ERYNNVVSVW
SKTNEELTNK MMEILKKDRD GFNVIYMMAD SGARGSRNQI RQLAGMRGLM AKTSGDIIEL
PIISNFKEGL SVIEFFISTN GARKGLADTA LKTADAGYLT RRLVDIAQDV VVRIEDCGTI
NGIKVEALKN GEEIVEPLRE KAVGSYSIER IKSPITGEII LDVNEEITED KIKLLETVGI
DKLVIRSVLT CEAEHGVCQK CYGRDFSNNK PVNIGEAVGI IAAQSIGQPG TQLTMRTFHI
GGVAQAGSED DKIALKNSFI LNGLEGFNVQ VDGGLLFTRK GTLRVINVIY EEDIKDIKEF
KVLDSQKVIK GMPLFTSKDG IDVLSSHIGY VRIKDNKLMI VSEEQEISLK TGTKLEVNVG
DYVEAGRVIG TFDPFAEPII AEVRGKVKFK DIILGTTLKE EINLETGNIE KRITDQVFES
LDPRILIIND RGIEIASYVL PGDAYLQVED GQDIDIGDII AKLSKGSEKT QDITGGLPRV
NDLFETRIPK NLTEMAKVSG VVQFKAIQKG KRLINVLDEY GVEHKHYIPA GKHLLVRDGD
VVKAGDMLCD GRINPHDVLE ILGGISLQEF LLAEIQDVYR KQGVSINDKH IGVIIKQMMK
KVKIVSVGDT NFVYNQKVDK HTFYEQNKRV IEQGGEPAVA SPILIGITKA SLNIDSFISA
ASFQETTKVL TDASIAGSVD DLKGLKENVV IGHLIPTGTG MNLYKRVKVR ENSSSEM
