RPOC_LEPBP
ID RPOC_LEPBP Reviewed; 1433 AA.
AC B0SSI3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=LEPBI_I1971;
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=456481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris;
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(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; CP000786; ABZ98073.1; -; Genomic_DNA.
DR RefSeq; WP_012388944.1; NC_010602.1.
DR AlphaFoldDB; B0SSI3; -.
DR SMR; B0SSI3; -.
DR STRING; 456481.LEPBI_I1971; -.
DR PRIDE; B0SSI3; -.
DR KEGG; lbi:LEPBI_I1971; -.
DR HOGENOM; CLU_000524_3_1_12; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; LBIF456481:LEPBI_RS09735-MON; -.
DR Proteomes; UP000001847; Chromosome I.
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; 1.
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; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1433
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000141778"
FT REGION 1383..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1410..1433
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 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 1433 AA; 160647 MW; AEA248FACB70A913 CRC64;
MRNYNSFESI TIRLASPERI KEWSFGEVKK PETINYRTLK PERDGLFCEK IFGTTKDWEC
YCGKFKSIRY KGVVCDKCGV EVTHSKVRRE RMGHIELAAP VSHIWYYRSV PSRMGLLLDM
TINQLKSVLY FEKYVIIDPA DSGRNRGELI DEDEYHNYLD EYGDKFIAGI GGDAIKELLA
RIDVDAEARV IRQKIQDKNK ISDKRIFKRL EVLEAFRDSG NRPEWMVLDV VPVIPPELRP
MVQLEGGRFA TSDLNDLYRR VINRNNRLKR LLALKAPEII VRNEKRMLQE AVGALFDNSR
RKRTVKGKGN RPLKSISDML KGKQGRFRQN LLGKRVDYSG RSVIVVGPEL KYHQMGLPKK
MALELFKPFI MKRLVDLELA PNIKSAKKKI EAEDKEVFDV LETVVKEHPV LLNRAPTLHR
LGIQAFLPVL VEGKAIKLHP LVCHAFNADF DGDQMAIHVP LAPKAQLETW MLMLSPHNIL
NPANGQPICG PTQDIVLGIY YLTSEVKDAK GEGKFFTGLE EVMYAIETKT VEIRSKISVL
HEGKIIETTP GRLIFNQVMP KGYVYINRTL GDKETNKIIA DVYEKFGPGI TVVMLDEIKR
LGYRYATVFA PTISIDDIRV SPQKEGLVND ANKEVEKADM EYRKGIITNE ERRKKVIEIW
TKTNDRITEG MFKELEKDQA GFNPVYVMAA SGARGSKQQI RQLAGMRGLM AKPSGEIIEL
AIRSNFREGL GVLEFFISTH GARKGLADTA LKTADAGYLT RRLVDISQDV IVSEDDCGTK
ANITLGIVKE GENVIVSLAD RVFGRYTAED LVDPVTEKVV FPKDTLITRA LGQQIENLGY
DKIKVRSPLT CRSRHGICTK CYGMDMARLV PAEIGEAVGT IAAQSIGQPG TQLTMRTFHV
GGAASATIQE KEHKVPFRSL VKSINGRLVT NANGSKVFAR RGTIIVNRLI QEFNTESLSS
VRIVDGQRLE KGEVFASQVG ESIEQRITSD QAGTVSLIGT TLRILGDDIV IPVKIGTILK
SEEGQIVEEN KALAEFDPYN EVAVSETAGT IVWEDLEIGK NVRRDVDPKT SNIILKVVEQ
KKDRLVPKVI VGSDGYSVPV DALLQFQNGD KVREGDVIFK IPSVAEKTRD ITGGLPRVDE
LFEARRPKDA CTLAEIDGKI EDKGEIVKEK RILYILPDSP EQEKVKVAIP IGKQIRVRQG
DFVKRGDQLD EGNFDPHDIL AIKGPSALHE YLVSEVQEVY RLQGVHINDK HIEVVVRSML
RKVIITDSGD TSFVNQQQVD KFLFDEENDR VEQEGGSPAQ GTPVLLGLTK ASLNTESYFS
AASFQETTKV LTDAAIKGKT DNLMGLKENV IIGHMIPAGT GMKKYRDIEV FKEMPGDLDW
DLDSEEEEEE LSELSEAAPV STATLSKLVA EEDEDEDELE EEADDSDDED DDD
