RPOC_LEPBL
ID RPOC_LEPBL Reviewed; 1404 AA.
AC Q054E1;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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=LBL_0744;
OS Leptospira borgpetersenii serovar Hardjo-bovis (strain L550).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=355276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L550;
RX PubMed=16973745; DOI=10.1073/pnas.0603979103;
RA Bulach D.M., Zuerner R.L., Wilson P., Seemann T., McGrath A., Cullen P.A.,
RA Davis J., Johnson M., Kuczek E., Alt D.P., Peterson-Burch B., Coppel R.L.,
RA Rood J.I., Davies J.K., Adler B.;
RT "Genome reduction in Leptospira borgpetersenii reflects limited
RT transmission potential.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:14560-14565(2006).
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; CP000348; ABJ78304.1; -; Genomic_DNA.
DR RefSeq; WP_011669622.1; NC_008508.1.
DR AlphaFoldDB; Q054E1; -.
DR SMR; Q054E1; -.
DR KEGG; lbl:LBL_0744; -.
DR PATRIC; fig|355276.3.peg.938; -.
DR HOGENOM; CLU_000524_3_1_12; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
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..1404
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308849"
FT REGION 1381..1404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1382..1404
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 778
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 852
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 859
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 862
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1404 AA; 157534 MW; BC0CB56829989B89 CRC64;
MRSHNDFESI TIRLASPERI KEWSYGEVKK PETINYRTLK PEKDGLFCEK IFGTTKDWEC
YCGKFKSIRY KGVICDKCGV EVTHSKVRRE RMGHIELAAP VSHIWYYRSV PSRMGLLLDM
TVNQLKSVLY FEKYVIIDPA DSGRSRGELI DEEEYHGYLD EYGDKFVAGI GADAIKELLA
RIDVDAEARM IRQKIQDKDK ISDKRILKRL EVLEAFRDSG NRPEWMVLDI VPVIPPELRP
MVQLEGGRFA TSDLNDLYRR VINRNNRLKR LLALKAPEII VRNEKRMLQE AVDALFDNSR
RKRAVKGKGN RPLKSISDML KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KYHEMGLPKK
MALELFKPFI MKRLVDLDLA PNIKSAKKKV EAEDKEVFDV LEYVVKEHPV MLNRAPTLHR
LGIQAFLPVL VEGKAIKLHP LVCHAFNADF DGDQMAIHVP LTPKAQLETW MLMLSPHNIL
NPANGHPICG PTQDIVLGIY YLTSELPSEP GAPLKSFSNL DEVHYAIDRG VVEFRTKISV
YHQGKILETT PGRLIFNTIL PEGYAYVNRP LSDKETNRII ADVYDKYGPA KTVLMLDDIK
KLGYRYATLF VPTISIEDIR VSPGKVGLVG DANKEVEKAD SEYRKGIITN EERRKKVIEI
WTKTNDLITE SMFKELEKDK GGFNPVFIMA ASGARGSKQQ IRQLAGMRGL MAKPSGEIIE
LAIRSNFREG LSVLEFFIST HGARKGLADT ALKTADAGYL TRRLVDISQD VIISEDDCGT
EESISLGIVK EGENVIVSLN DRVFGRYTAE DVIDPVTDKV VYPRNTLITR EVGQKVENLG
YDKIRVRSPL TCESKQGVCI RCYGMDMARL IPAEIGEAVG TIAAQSIGQP GTQLTMRTFH
IGGAASAKVQ EKEHKVSYTG IVNNINGRLI TNEKSQSVFS RRGSIVIQRL IQQYKTEELS
NLRVENGQKV DKGELVATSP SGENITSAMP GAVHIENGIF RILGEEAVIP VKTGTVVNVK
VNDITQPNQP LAEFDPYNEV GISEIDGTVQ WMDLEIGKNV RRDEDLRTSN ILLKVIEQRR
EKLNPRIAVI SGGSREEYSV PVDAIISVQD GDKVKAGDIL FKIPTVAEKT RDITGGLPRV
DELFEARRPK DATTLAETDG KIEISGEIVK EKRVLYIHPD NPDQEKVKVT IPIGKQIRVR
NGDFVKRGDQ IDDGNLDPHD ILRVKGVTAL QVYLVQEVQE VYRLQGVHIN DKHIEVVVRQ
MLRKVLITDS GDTSFVNQQQ IDRLMFNEEN KRVIAEGGSP AESVPILLGL TKASLNTESF
FSAASFQETT KVLTDAAIKG KTDNLMGLKE NVIIGHMIPA GTGTKKYKDI SVFKSAYGDL
DRPLEEEEEE EIPQSIADDS DGDE
