RPOC_DEIGD
ID RPOC_DEIGD Reviewed; 1537 AA.
AC Q1J0P7;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
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=Dgeo_0635;
OS Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=319795;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11300 / AG-3a;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL Submitted (APR-2006) 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; CP000359; ABF44937.1; -; Genomic_DNA.
DR RefSeq; WP_011529778.1; NC_008025.1.
DR AlphaFoldDB; Q1J0P7; -.
DR SMR; Q1J0P7; -.
DR STRING; 319795.Dgeo_0635; -.
DR PRIDE; Q1J0P7; -.
DR EnsemblBacteria; ABF44937; ABF44937; Dgeo_0635.
DR KEGG; dge:Dgeo_0635; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_0_0; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002431; 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; 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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1537
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000308832"
FT REGION 1502..1537
FT /note="Disordered"
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 746
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 748
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 750
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1120
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1208
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"
SQ SEQUENCE 1537 AA; 170603 MW; 351B417D31432811 CRC64;
MKDFSKVRIA IASPAKIREW SFGEVEKPET INYRTLKPER EGLFDERIFG PIKDYECACG
KYKRQRYEGK VCERCGVEVT SSKVRRYRMG HIDLATPAAH IWYVKDTPSK IGTLLDLSAA
QLEKVLYFSS FLVTDPRNAQ KDGRPLRRGE LLSDDEYREL RFGRQETYTL PSGTEAAVRD
GEYVTRGQVL GGNVVSKMDG LAQYRFPRRA EIAYAEEAEA SLPLPSDVLV QQDSFRPGEI
LAELEGDVQI TAPVDGTAFL LDMGEDSVLV ELRDSAAEDA AQGEVLARVY IPHGMNVQVA
EGEVVEAGSV LATAAAGDRL RVSRDSRLSN VNFPKKKGDV KVTAHWTRRV EYRIEPQMHV
LVGDGSEVRK GQKVVGAIDK EEEVIAEADG VITLHAPASI IVSKARVYAY QDEPLVVNGD
RVEPGDELAD SGNLRSEISG RVEIDLVRKQ VRVIESYDFE AKMGAEAVKE LLDDLDLDQL
EAELSEQMKD NSRHKRAKAR KRLEVVRAFK RSGNHPSWMI LETVPVMPPD LRPMVQVDGG
RFATSDLNDL YRRLINRNNR LKKLIGQGAP DMIIRNEKRM LQEAVDALID NGRRGSPVTN
PGSDRSLRSL TDLLGGKQGR FRQNLLGKRV DYSGRSVIVV GPQLKLHQCG VPKRMALELF
KPFLFKVLEE KGEVTNIKQA RKMLERYRDT RDSVWDALEE VIEDKVVLLN RAPTLHRLGI
QAFEPVLVEG QSIQLHPLVC EAFNADFDGD QMAIHVPLSA QAQAEARIQM LSAHNLLSPA
NGEPNVKPSR DIILGIFTLT QLRKDNLGAG SEFANEQDAL KALDEGRVAL NTPIRVNGVE
TSPGRLKYVF SSPDEAIMAV DRGEIDYQDH VRIRLNGTVY ETSAGRVMFR RLVQEALGAQ
GHLVDTLVNL DTAYEKDSLK DMVMACYKEL GIEATAGLLD ALKDSGFKLS TISGITIGID
DIVLPPNKRE LLAEADEKLA AIEQNYEFGF MTDEERYKQV VQLWNDTTDE VKNAVFENFS
RNYPFNPLWI MSQSGARGNP QQIRQLAGMR GLMARPDGST IEVPIRASFR EGLTVLEYFI
STHGARKGGA DTALRTADSG YLTRKLVDVA HEVVVRDVDC GTTDYTVMPL GTTDERTGEW
RTRKGSEIET AIYGRTLTAD VELSDGRVIP AGQMLSLEDV KAITRDAKAI GEVFVRTPLN
CRVRAGVCQK CYGYDLSQAK PVSLGEAVGV VAAESIGEPG TQLTMRTFHT GGVAGGGDIT
MGLPRVIELF EARKPKTQAV VADRDGVVRI EEEEERYLVR IEAEDEAFSS KTPMKISKSL
RLIVRDGDHV EAGQPLTRGA INPHDLLLYK DTDAAQRYLV EEVQRVYRSQ GVKVHDKHIE
VIVRQMLRYV EITDGGDTDL LEGQTVERWE VDQANDALPE GKTPASWKPV LLGITKSSLT
TKSWLSAASF QHTTHVLTEA SMRGQVDELI GLKENVILGK LIPAGTGLTT VREMQVADER
TLEKYGQTSV STDAVTGSQR YDDTRPSSTS INPSYGD
