RPOC_DEIRA
ID RPOC_DEIRA Reviewed; 1546 AA.
AC Q9RVW0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=DR_0911;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
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; AE000513; AAF10485.1; -; Genomic_DNA.
DR PIR; F75461; F75461.
DR RefSeq; NP_294635.1; NC_001263.1.
DR RefSeq; WP_010887556.1; NZ_CP015081.1.
DR AlphaFoldDB; Q9RVW0; -.
DR SMR; Q9RVW0; -.
DR STRING; 243230.DR_0911; -.
DR PRIDE; Q9RVW0; -.
DR EnsemblBacteria; AAF10485; AAF10485; DR_0911.
DR KEGG; dra:DR_0911; -.
DR PATRIC; fig|243230.17.peg.1098; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR InParanoid; Q9RVW0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002524; 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; 2.
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..1546
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067739"
FT REGION 1512..1546
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1517..1536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 72
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 756
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 758
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 760
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1130
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1546 AA; 171361 MW; 2FE3CEA739704C75 CRC64;
MKDFNKVRIA IASPEKIREW SFGEVEKPET INYRTLKPER EGLFDERIFG PIKDYECACG
KYKRQRYEGK VCERCGVEVT SSKVRRYRMG HIDLATPAAH IWYVKDSPSK IGTLLDLSAG
QLEKVLYFSS FIVTKPFNAQ KDGRPLKRGE LLSDDEYREL RFGRQETYTI PNSVEDVEIR
DGEYVTRGQI LGGNVVSKMD GLAQYRFPRR AVIAYSEGVE ASLPLPADTL VEQETFRAGE
ILAELEQDVQ ITAPVAGTVF MHDLGEDSVM IELREGVEAN DSDEEEAADP IRGEVLARVY
VPHGMNVQVA EGEVIEAGAL LADASEGARL RVSRDSNLSG VTFPKKKGDV TVTAHWTRRV
EYPIDPTMHV LVGDGSEVTK GQRVIGAIDK EEEVIAEADG VITLHQPASI LVSKAKVYAY
DDEPLVVNGD RVEPGDELAD DGNLRSEISG RIELDLVRKQ VRVIESYDFE AKMGAEAVKE
LLDELNLDEL ETELNEQMKD NSRHKRAKAR KRLEVTRSFK ASGNNPSWMI LGTVPVMPPD
LRPMVQVDGG RFATSDLNDL YRRLINRNNR LKKLMSQGAP DMIIRNEKRM LQEAVDALID
NGRRGSPVTN PGSDRSLRSL TDLLGGKQGR FRQNLLGKRV DYSGRSVIVV GPQLKLHQCG
VPKRMALELF KPFLFKVLEE KGEVTNIKQA RKMLERYRDT RDSVWDALEE VIEDKVVLLN
RAPTLHRLGI QAFEPVLVEG QSIQLHPLVC EAFNADFDGD QMAIHVPLSA QAQAEARIQM
LASHNLLSPA NGEPNVKPSR DIILGIFTLT QLRRDNLGAG TEYASEADAL AAFDEGKLSL
NSPVMVNGVE TSPGRLRYTF SNPDEALHAV EQGEIDHQDH VRIRLNGQVY ETSAGRVQFR
RMVQEALGAQ GGLIDTLVDL ETTYEKDALK DMVMACFKHL GIEATAGLLD GLKEGGFKLS
TTSGITIGID DIVLPPNKGE LLAEADQMLA EIEQNFEFGF MTEEERYKQV VQLWNNTTDA
VKDAVFENFS KNYPFNPLWI MSQSGARGNP QQIRQLAGMR GLMARPDGST IEVPIRASFR
EGLTVLEYFI STHGARKGGA DTALRTADSG YLTRKLVDVA HEVVVRDVDC GSTDSTVMPL
GATDERTGEW RSRKGSEIET SIYGRTLTAD VEFSDGRVIP EGEMLSMEDV KAIAKDAKHI
GEVFVRTPLN CRVKAGVCQK CYGYDLSQAK PVSMGEAVGV VAAESIGEPG TQLTMRTFHT
GGIAGGGDIT MGLPRVIELF EARKPKTQAV VADRDGVIRI EEEEERYLVR IEADDEQYSS
KTATKVPRVL RMTVKDGERV EAGQPITRGA VNPHDLLMYK DTDAAQRYLV EEVQRVYRSQ
GVKVHDKHIE VIVRQMLRWV EVTDGGDTTL LEGQTVEHWE VDQANEALAE GQTPASWKPV
LLGITKSSLT TKSWLSAASF QHTTHVLTEA SMRGQVDDLI GLKENVILGK LIPAGTGLLT
VREMQVADDR TLEKYGEGST SSDAVTGGQR YDDTRPGSSI NPGYGD
