RPOC_THEM4
ID RPOC_THEM4 Reviewed; 1649 AA.
AC A6LKB7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Tmel_0501;
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=391009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-2007) 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; CP000716; ABR30368.1; -; Genomic_DNA.
DR RefSeq; WP_012056729.1; NC_009616.1.
DR AlphaFoldDB; A6LKB7; -.
DR SMR; A6LKB7; -.
DR STRING; 391009.Tmel_0501; -.
DR PRIDE; A6LKB7; -.
DR EnsemblBacteria; ABR30368; ABR30368; Tmel_0501.
DR KEGG; tme:Tmel_0501; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000001110; 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; -; 2.
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; 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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Transcription; Transferase; Zinc.
FT CHAIN 1..1649
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353448"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 65
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 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 747
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 751
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1078
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1269
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1649 AA; 185605 MW; D60382419EC2E27E CRC64;
MMGSTFKRKI SKVTVKVASP EVIRSWSSGE VKKPETINYR TFKPEKDGLF CEKIFGPTKD
YECACGKYKG KKYEGTVCER CGVRVESKEA RRKRMGHIDL FAPVVHVWYL KSSPSILSSL
LGIQAKELEN VIYYGGKRII EKILIVTNPK DTDFIKGSLL YQTEYEIYNQ KLDFEVMPGV
IIKSPVAPVI SSISGEVKIR HEKTHTDREI TWVDVRKISR AEHRVYNGMV LNVKNGDYVN
QGDEIVSEMQ IDPIYAPFDG TVEIDEISNT ITIKPLTTSK DMPVTFSLPY GVKPVVPNNS
KVKKGDQLTN GTVLPAVIAS VSGNISFGKE LNVRPLEDGK YEVLTSGSVY VENVVEEKHY
PLFEGAFVYV KDGDEISEGQ TIADRFLFED EYLTLDEYKI FEQHYPAMFT AESEVENDRP
IVVITEIDDE VSVETGLKIG DIITDHQYSA YRTLYNDKIE ADSGASAIKK LLQKLDLEKL
KAEIESELKK VSKSSGRAKK LLRRLKIVKD LLKSETKPEW MILEAIPVVP PDIRPMIQVE
GGRFATTDLN DLYRRVINRN NRLKKLYEMN SPEIIIKNEK RMLQEAVDSL IYNGRMGKAV
TDRNGRALKS LTDLLKGKKG RFRRNLLGKR VDYSGRAVIV VGPHLKIHEC GLPKKMAMEL
FKPFVLAELL NKDDETSKTA RKMKKAIIEK EMPQAYEVLE EIIKGHPVLL NRAPTLHRMS
LQAFEPKLIE GNAIQLHPLV CPPFNADFDG DQMAVHVPLS AAAQAEAKFL MLSRYNIISP
AHGKPISMPG KDIVAGVYYL TMVGKDYDKV QKENIKWKFS SIDEAELAYE FGHIRLHDPI
LVKVDDRVIK TTYGRLVFAN IVPREFRDYN KTYGKGAIKD LVYKTFKKYG VDRTADLLDD
IKDLGFHYAT ISGLTVSITD FYISPERRRI IDEAKKKISE VEELFALGFL SDEERYRETI
KIWADATEKV QDATFEYIGK DPFNPVYIMV DSGARGNKDQ LKQLAGMRGL MADPSGRTIE
IPIISNFREG LSVLEFFIST HGARKGSADT ALRTSSAGYL TRRLVDVAQS VVITTTDCGT
ENGVRATVLK SSDGLTVEKL EDFLFGRVLA KDVYDPKTNS VLVNPENGKE YTRDTMIDDD
DAKFLGNYSV RIPVSRELEI NLTNPELPEN YCELITDFIY DGVHYDEGTE VNWDIIRKAK
NSGLEKLTVK EYPIVGKVSV ETVVSQKDIK QLVVDEELIM PTTAKILEGH NVESVQVRPE
IIVRSVLTCE AEHGVCSKCY GMDLSNHKII GVGEAVGVVA AQSIGEPGTQ LTMRTFHTGG
IATTADITQG LPRAEELFEA RKKLKEPEGI FSRVKGYVKD IVEDETGKKK VYIEDEAGDI
HEYDIPTKVK VSVNKGQKIL PGQSLSTGAI RPRKILETLD VDTTALYLLK EIKKVYVEQG
VDIHDKHFEI IIKQMLDKVE VIDPGDTDYL PGDLLRLQMV KRINKQILEE NVHVETNRKR
VIGKILHQHL IAEDENGEIV EIAPEGVEVT EEILEKAIKS GIKEIIVKNG DGEIVTYQIL
PKEPIKYRRR LLRITKASLE RVGWLSAASF QQTPQVLTEA AIEGSVDHLL GLKENVIVGQ
LIPAGTGLDM FANIQIEETP RLAQKEKMA
