RPOC_FRAP2
ID RPOC_FRAP2 Reviewed; 1416 AA.
AC B0TX11;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 86.
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=Fphi_1047;
OS Francisella philomiragia subsp. philomiragia (strain ATCC 25017 / FSC 153 /
OS O#319-036).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=484022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25017 / FSC 153 / O#319-036;
RG US DOE Joint Genome Institute;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Richardson P.;
RT "Complete sequence of chromosome of Francisella philomiragia subsp.
RT philomiragia ATCC 25017.";
RL Submitted (DEC-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; CP000937; ABZ87269.1; -; Genomic_DNA.
DR RefSeq; WP_012280434.1; NC_010336.1.
DR AlphaFoldDB; B0TX11; -.
DR SMR; B0TX11; -.
DR STRING; 484022.Fphi_1047; -.
DR PRIDE; B0TX11; -.
DR EnsemblBacteria; ABZ87269; ABZ87269; Fphi_1047.
DR KEGG; fph:Fphi_1047; -.
DR eggNOG; COG0086; Bacteria.
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..1416
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353367"
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 1416 AA; 157279 MW; 1C12D74322C17F66 CRC64;
MNNGILHQNY NSKKFDIIKI SLASPEVIRS WSHGEVKKPE TINYRTFKPE RDGLFCAKIF
GPIKDYECLC GKYKRLKHRG VVCERCGVEV EQAKVRRERM GHIDLVCPVV HIWYLKSLPS
RIGLFLDMPL KNVEKVLYFE SYIVTDPGMT PLEKKQLLTD DEYAEALENY GYEFEASMGA
EAIRDLLADT DLETEIESLQ AEYEESKSTA KKEKAIKRLR LLETFQASGN KPEWMVMTVL
PVLPPDLRPL VPIEGGRFAT SDLNDLYRRV INRNNRLKKL LDLNAPDIIV RNEKRMLQEA
VDALLDNGRR GRAVTGSNKR PLKSLADMIK GKQGRFRQNL LGKRVDYSGR SVITVGPSLR
LHECGLPKKM ALELFKPFVY SKLRLGGYAT TIKQAKRMVE LEEAVVWDIL EVVINEHPVL
LNRAPTLHRL GIQAFEPKLI EGKAIQLHPL VCAAFNADFD GDQMAVHVPL TVESQLEARV
LMMSTNNILS PASGQPIITP TQDIVLGLYY ITREKEGARG EGKLFSNYDD VSRAYNSGTI
DIHAKIKLRI DRQVFDTKGN TYNEKGVVNT TVGRALLLNI LPEGLSFSLL NKVLVKKEIS
KIINQAFRVL GGKATVVLAD KLMYAGFKYS TLSGVSVGVD DMTIPENKEA KVEEAEKEIK
HITEQYQSSL ITENERYNNI INIWSKTSDE VGASMMDAIS KDTVMVNGEN KEIESFNSVY
MMAKSGARGS YNQMRQLAGM RGLMAKPDGT MIETAITANF REGLSVLQYF TSTHGARKGL
ADTALKTANA GYLTRRLVDV AQDLVVIEED CGTDDGLMFS AIVEDGEVKV PLVERALGRT
LAADVVTEKG VVLLEAGTLL DENLVEILDD NGIDMIKVRS PITCKTRRGL CAKCYGRDLA
RERKVNVGES VGVIAAQSIG EPGTQLTMRT FHTGGAASLG ITVSDIKVKT AGKIKFKNIR
TVTNKDGQNI VISRAGEIIV SDTMGRVREQ HKIPMGAVVP LASGKGVEIG DVIATWDPHA
QPLITDVAGK VVLEDVIDGI TSKHTYDDLT GQQTIEITSI SQRTTSKNLK PVVKVVDEKG
NEIKSISLAV GAVLNVTDDS VLEVGDVVAK IPLEGSKNKD ITGGLPRVAE LFEARRPKDA
AILSPCDGMV RLGNRDTKEK QRIEILDKSG HIAEEILLPK SRHLVVFDGE QVSKGDVLAD
GPTDPHDLLK YKGLEAFADY ILIEAQSVYR MQGVVINDKH IETIVRQMLR KATILDEGDS
KFVKDESIEL VRILEENDRL AKEGKRLVEY ELTLMGITRS SLSTESFLSA ASFQETTRVL
TEASIHSQVD QLRGLKENVL IGRLIPTGTG LAVRKESNKI EKMREELGVE DNMIFTEASS
FNTEDTLFEN QIEKEDKDIN DDIEESLRNA LESLDF
