RPOC_THENN
ID RPOC_THENN Reviewed; 1690 AA.
AC B9KBJ4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=CTN_0214;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-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; CP000916; ACM22390.1; -; Genomic_DNA.
DR RefSeq; WP_012645100.1; NC_011978.1.
DR AlphaFoldDB; B9KBJ4; -.
DR SMR; B9KBJ4; -.
DR STRING; 309803.CTN_0214; -.
DR PRIDE; B9KBJ4; -.
DR EnsemblBacteria; ACM22390; ACM22390; CTN_0214.
DR KEGG; tna:CTN_0214; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_0; -.
DR OMA; EHEIIAN; -.
DR Proteomes; UP000000445; 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..1690
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_1000165857"
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 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 755
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 757
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1302
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1690 AA; 191027 MW; A93C6E5821B8846E CRC64;
MPMSSFKRKI KAIQIKIASP DVIRSWSGGE VKKPETINYR TFKPERDGLF CERIFGPVKD
YECACGKYKG KKYEGTVCER CGVRVESREA RRKRMGHIEL AAPAVHIWYL ESIPSVLGTL
LNMNVSDLEN IIYYGSRRVI ERAFIVTDPK DTPFAQGDII YETEYRIYRK KWDFEVEQAF
IVKNPRSPVL SDIDGEVILR TEKTVTGREI TWIIVRNVNR AEHTVLPGMI ITVKDGQEVE
KGQDLTREMN VDPLYAPFDG HVEIDEISNT ITVKPLTTSK DQPVVFTVPY GARVLVSNGQ
KVKKGDQLTT STTLPAVKAS ISGRVKFGSN LNVRALEDGN FEVLSSGNVY IEQVIEERKY
PVFEGALVYV NNGDQVKKGD HLADRFLFEE EYLSSTEYKI FESHYPTMFD VEERTENDRP
IVVITDIDPE VSKETGLKMG DIITENEYEA YLQIYPEKIV ADAGAQAIKK LLQNLDLEEL
RAELEAELKK LPASSSKAMK LRRRLKMVKD FIKSGNKPEW MVLEVVPVIP PDLRPMIQIE
GGRFATTDLN ELYRRLINRN NRLRKLLELG APEIILRNEK RMLQEAVDAL IHNGSDSEGK
RSRRAVLKDR NGRPLKSLTD LLKGKKGRFR RNLLGKRVDY SGRAVIVVGP HLKIHQCGIP
KKMAMELFKP FVLAKLLGEG STSKTMRKVK KAIIEKEMPE AWEVLEEVIK GSVVLLNRAP
TLHRMSIQAF EPKLVEGNAI QLHPVVCPPF NADFDGDQMA VHVPLSAAAQ AEARFLMLSR
YNIISPAHGK PISLPTQDII IGSYYLTTVG KDFDSLKEED IRWRFSSPEE AMLAYHLGYI
KLHTPILIKV SIKGEEKRIK TTLGRVIFNS ILPEDLRDYN RIFDKKQINA LVYETFKRYG
IDRAADLLDD VKDLGFHYAT VSGLTLSLKD LKIPPERDEI LKRTWEKVRI IEENYERGFL
TEEQRKSEII RLWMNVTEEI TELTSKTLAE DPFNPIYMMV NSGARGNIDQ VKQLAGIRGL
MIKAYDPRSR EIKSKIFKGQ AIHEALTFDY PVDKNLREGV DILQFFISTY GARKGQVDTA
MNTSFAGYLT RRLVDVAQSV TVTEPDCGTH EGIRAMDLIK DGTVVEKMNE FLFGRVLASD
VLDPETKEVL KNPETGKEYT RNTMLTDDDA NFLASYKKMV DVVKYDEIDI TELSLPNMYA
EIAEPVGEYK EGTELTWDVV KAARNEGKYR IKVKMYPVVG TVYANEQPLY DKKGERELLV
YQEVINEVVA KLLEENGVEK VLVRPDIIVR SPLTCESEYG VCAACYGMDL SNHKIVNVGE
AVGIVAAQSI GEPGTQLTMR TFHVGGVMGA SDIVSGLTTV EKTFEPYAFL REEKSGGKKE
IRKYYGSEAV LCEVDGFVKD IATDETGRTV IYIEDYAGGI HAYRIPKRAK VKVKKGQKVL
RGDTLTTGAI VWWKLLELES EKGVLTAMNL LKIIKNAYVQ QGVSIHDKHF EIIFRQMLSM
ALVIDPGDSD YLPDQLVPLV DIKRTNREIL EGNARVEENR KWVIGKMLAK RVITETDDGE
LVELAQKGEE VTEELLKKFI EAGIKEIDVV EKDRVVTYQI LPKEPIKYKR RLLSLKKAAL
NYPGWLSAAA FEETAWVLTA AAIEGKVDPL IGLKENVIVG QLIPAGTGLD VFAGIQVEET
PRAAAEEKLA
