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RPOC_CLAM3
ID   RPOC_CLAM3              Reviewed;        1299 AA.
AC   A5CUC6;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, 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=CMM_2630;
OS   Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC   Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX   NCBI_TaxID=443906;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCPPB 382;
RX   PubMed=18192381; DOI=10.1128/jb.01595-07;
RA   Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA   Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA   Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA   Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA   Bartels D.;
RT   "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT   michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT   in pathogenicity.";
RL   J. Bacteriol. 190:2138-2149(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; AM711867; CAN02713.1; -; Genomic_DNA.
DR   RefSeq; WP_012039319.1; NC_009480.1.
DR   AlphaFoldDB; A5CUC6; -.
DR   SMR; A5CUC6; -.
DR   STRING; 443906.CMM_2630; -.
DR   EnsemblBacteria; CAN02713; CAN02713; CMM_2630.
DR   GeneID; 56886974; -.
DR   KEGG; cmi:CMM_2630; -.
DR   eggNOG; COG0086; Bacteria.
DR   HOGENOM; CLU_000524_3_1_11; -.
DR   OMA; YRNIRVE; -.
DR   OrthoDB; 4421at2; -.
DR   Proteomes; UP000001564; 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; 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; Transcription; Transferase; Zinc.
FT   CHAIN           1..1299
FT                   /note="DNA-directed RNA polymerase subunit beta'"
FT                   /id="PRO_0000308829"
FT   REGION          188..209
FT                   /note="Disordered"
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         535
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         537
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         539
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         882
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         959
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         966
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT   BINDING         969
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ   SEQUENCE   1299 AA;  143266 MW;  FDBD7DBDFA101957 CRC64;
     MLDVTTFDEL RIGLATADDI RRWSHGEVKK PETINYRTLK PEKDGLFGEQ IFGPSRDWEC
     SCGKYKRVRF KGIVCERCGV EVTKSAVRRE RMGHIELAAP VTHIWYFKGV PSRLGYLLDM
     APKDLEKVIY FAAYMVISVD EDARHEDMPG LENELRLEIK TLQDQRDSQI AERLGRLETD
     LAALEAEGAK SDQKRRAKDG AEKEMGQTRK AFDEDISRLE RVWEEFRSLK VGELKPEDAV
     FHELQDRFGI YFEAHMGAEA IQKRLEAFDL EAEGELLREQ IATGKGQKKI RAIKRLRVVS
     SFLATGNSPA AMVLQVVPVI PPELRPMVQL DGGRFATSDL NDLYRRVINR NNRLRRLLDL
     GAPEIIVNNE KRMLQEAVDA LFDNGRRGRP VTGTGNRALK SLSDMLKGKQ GRFRQNLLGK
     RVDYSGRSVI IVGPQLKLHQ CGLPKQMALE LFKPFVIKRL IDLSHAQNIK AAKRMVERSR
     GQVWDVLEEI IRERPVLLNR APTLHRLGIQ AFEPQLVEGK AIQLHPLVCA AFNADFDGDQ
     MAVHLPLSVE AQAEARILML ASNNILKPSD GRPVTLPTQD MIIGLHHLTT LKEGVAGEGR
     AFSSVAEAIL AKDQLSLDLN AKVRIRLHDI YFGEGEAPEG VELDEKGKTV GPVLLETTLG
     RALFNETLPV DYPYIEAVAD KGKLSEIVND LAERYPKVEV AAALDRIKDA GFYWATRSGV
     TVALSDVLTP PTKAAILSGY EKQAAKVQGQ FEKGLTTNAE RRQELIEIWN KATAEVAKAM
     EDNLPADNNI NRMVSSGARG NWMQVRQIAG MRGLVSNPKG EIIPRPIVHS YREGLTVAEY
     FISTHGARKG LADTALRTAD SGYLTRRLVD VSQDVIIRED DCGTGRGLDL PIATKGADGS
     SVRDSNVENS VYARSLAADA VNEAGEVVAP AGSDVGDVMI DHLIAAGVHE IKVRSVLTCE
     SAVGVCAACY GRSLATGKLV DIGEAVGIIA AQSIGEPGTQ LTMRTFHTGG VASADDITQG
     LPRVQELFEA RTPKGASPIA EAAGRITIED TDRSRKVILT PDNGDEPHIY PVLKRATLLV
     EDGQHVELGQ QLHVGAIDPK EVLRVKGVRE VQKHLVGGVQ GVYRSQGVPI HDKHIEVIVR
     QMLRKVTVVE HGDTDLLPGE LVDRARYNEV NRATLTEGKK TASARQEVMG ITKASLATES
     WLSAASFQET TRVLTQAAME GKSDPLMGLK ENVIIGKLIP AGTGLAKYRD VTVTATEEAK
     AERYPNRIFT DESVFNESDL SFVDFDSFSS DDYTPGTYN
 
 
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