RPOC_FRATM
ID RPOC_FRATM Reviewed; 1417 AA.
AC B2SFD7;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=FTM_0210;
OS Francisella tularensis subsp. mediasiatica (strain FSC147).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=441952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSC147;
RX PubMed=19521508; DOI=10.1371/journal.ppat.1000472;
RA Larsson P., Elfsmark D., Svensson K., Wikstroem P., Forsman M., Brettin T.,
RA Keim P., Johansson A.;
RT "Molecular evolutionary consequences of niche restriction in Francisella
RT tularensis, a facultative intracellular pathogen.";
RL PLoS Pathog. 5:E1000472-E1000472(2009).
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; CP000915; ACD30290.1; -; Genomic_DNA.
DR RefSeq; WP_012429131.1; NC_010677.1.
DR AlphaFoldDB; B2SFD7; -.
DR SMR; B2SFD7; -.
DR PRIDE; B2SFD7; -.
DR KEGG; ftm:FTM_0210; -.
DR HOGENOM; CLU_000524_3_1_6; -.
DR OMA; YRNIRVE; -.
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; 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.
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..1417
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353369"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 83
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 811
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 884
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 894
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1417 AA; 157416 MW; 43BAE975B7CB19B6 CRC64;
MNNGILHQNY NSKKFDIIKI SLASPEVIRS WSHGEVKKPE TINYRTFKPE RDGLFCAKIF
GPIKDYECLC GKYKRLKHRG VVCERCGVEV EQAKVRRERM GHIDLVCPVV HIWYLKSLPS
RIGLFLDMPL KNVEKVLYFE SYIVTDPGMT PLEKKQLLTD EEYAEALENY GYEFEASMGA
EAIRDLLADT DIESEIELLQ AECEESKSTA KKEKAIKRLR LLETFQASGN KPEWMVMTVL
PVLPPDLRPL VPIEGGRFAT SDLNDLYRRV INRNNRLKKL LDLNAPDIIV RNEKRMLQEA
VDALLDNGRR GRAVTGSNKR PLKSLADMIK GKQGRFRQNL LGKRVDYSGR SVITVGPSLR
LHECGLPKKM ALELFKPFVY SKLRLGGHAT TIKQAKRMVE LEEAVVWDIL ETVINEHPVL
LNRAPTLHRL GIQAFEPRLI EGKAIQLHPL VCAAFNADFD GDQMAVHVPL TVESQLEARV
LMMSTNNILS PASGQPIITP TQDIVLGLYY ITREKEGARG EGKLFSSYED VSRAYNSGTI
DIHAKIKLRI DRQVFDTKGN TYNEKGVVNT TVGRALLLNI LPEGLSFSLL NKVLVKKEIS
KIINQAFRVL GGKATVVLAD KLMYAGFKYS TLSGVSVGVD DMTIPDNKEA KIEEAEKEIK
QITEQYQSSL ITENERYNNI INIWSKTSDE VGASMMDAIS KDTVSINGEK KEIESFNSVY
MMAKSGARGS YNQMRQLAGM RGLMAKPDGT MIETAITANF REGLSVLQYF TSTHGARKGL
ADTALKTANA GYLTRRLVDV AQDLVVIEED CGTDDGLMFS AIVEDGEVKV PLVERALGRT
LAADVVTEKG VVLLEAGTLL DENLVELLDD NGIDMIKVRS PITCKTRRGL CAKCYGRDLA
RERQVNVGES VGVIAAQSIG EPGTQLTMRT FHTGGAASLG ITVSDIKVKT AGKIKFKNIR
TVTNKEGQEI VISRAGEIIV SDTMGRVREQ HKIPMGAVVP LASGKAVEIG DVIATWDPHA
QPLITDVAGK VVLEDVIDGI TSKHTYDDLT GQQTIEITSI SQRTTSKNLK PVVKIVDEKG
AKLKSIPLAV GAVLNVADDS ILEVGDIVAK IPLEGSKNKD ITGGLPRVAE LFEARRPKDA
AILSPCDGMV RLGNRDTKEK QRIEIIDKNG HIVEEILLPK SRHLVVFDGE QVSRGDVLAD
GPTDPHDLLK YKGLEEFADY ILIEAQSVYR MQGVVINDKH IETIVRQMLR KAVILDEGDS
KFVKDESIEL VRILEENDKL RKQGKKEVEY ELVLMGITRS SLSTESFLSA ASFQETTRVL
TEASINSQID NLRGLKENVL IGRLIPTGTG LAVRKESAKI EKMREELGVE DNMVFTDLSS
FNPEEISFDS IQSQKEDKDI NEDIEESLRN ALESLDF
