RPOC_MESFL
ID RPOC_MESFL Reviewed; 1254 AA.
AC Q6F0L8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=Mfl597;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) 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; AE017263; AAT75955.1; -; Genomic_DNA.
DR RefSeq; WP_011183495.1; NC_006055.1.
DR RefSeq; YP_053839.1; NC_006055.1.
DR AlphaFoldDB; Q6F0L8; -.
DR SMR; Q6F0L8; -.
DR STRING; 265311.Mfl597; -.
DR PRIDE; Q6F0L8; -.
DR EnsemblBacteria; AAT75955; AAT75955; Mfl597.
DR GeneID; 2897589; -.
DR KEGG; mfl:Mfl597; -.
DR PATRIC; fig|265311.5.peg.601; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000006647; 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; 1.
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.
DR TIGRFAMs; TIGR02386; rpoC_TIGR; 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..1254
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225550"
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 61
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 501
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 871
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 946
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 953
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 956
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1254 AA; 139622 MW; 007379CCE3DED039 CRC64;
MENKNNKVIK IELASADTIR SWSHGEVTKP ETINYKTLKA EKDGLFDEKI FGPTKNYECF
CGKFKKANPM NKGKKCEKCG VELTESIVRR ERMGHIELAE PVTHIWMVKV SPSRIASLLD
LKSKELEEVV YFVSHIVLDP GTSKHFAAKE VLDLGVSKSQ KTRSKLRPAI EEIVTLINDP
AHRDTLKAER LLEELNNPTI PFSIDEATAL ISKYTDAKFG IGASAIEELL KQIDLDKEIE
ITKNTLDAIG PNADNSKLLK RLDILESLKR SNQKPEWMVL RVLPVIPPDI RPIIQLDGGR
FTTSEINDLY RRIIIRNERL LKVKEMGAPS IIINNEKRML QEAVDALLDN ERKPRPIQGK
DKRPLKSLTS VLKGKQGRFR QNLLGKRVDY SGRSVIAIGP DLKMYQAGIP REMALTLFKP
FVIQWLQEHE YAENVKVAEK MILQNDPKIW EALEHVIKDR PVLLNRAPTL HRLGIQAFEP
KLVKGKAIRL HPLVTTAFNA DFDGDQMAVH VPITKEAVAE ARALMLGSNA ILGPKDGKAI
VTPGQDIILG NYYATFEEKG QLGEGTMFAE ITEAINAFDT GIVSLNAVIG IAVDALPAEK
FTEEQRKGYL LTTVGKILFN QIFDASFPWI NSSSIYDAKE AVNSFIFDFS KDINEAIAEY
TIVTPIKKKE LSIIIEIYFN KFGARKTAEM LDKMKDLGFK YSTKSGTTIS AGDVVAFKHK
YEEFAEADQK VAEITSFYNE GMLTKEEKKH RVIEVWSDVK DDIQKRLELV LKQDTKNPVF
VMADSGARGN VSNFTQLVGM RGLMNDTKGD IKEIPIKSSF REGLSVSEYF VSTHGARKGM
ADLALKTADS GYLTRRLVDV SQEIVVVNED CKANKGFEIE SVIDTKHNNV IVPLKDRIVG
RYSFNDIKDI KGNVIVAKDT LIESKEADAI IAAGITKVTI RSVLTCDNQK GVCQRCYGRN
LATASLVKIG EPVGVIAAQS IGEPGTQLTM RTFHTGGVAG DADITQGLPR IKELLDVTTQ
KGSVAIIAEK AGVVSDIINK NGINTIVVTE EVNGTQIEKQ YKTMYNAVLR VNKGDQVKPG
KKLTEGSINL HDLLEVAGTT AVQNYILKEV QKVYRLQGIE ISDKYIEIIV KQMLNKVKVI
QSGESHLLQG EIVTQQKFKE VVTQCIREGL VPPVAKNQIL GIKKAPLKSE SWLSSASFQD
TARVLTDAII KGREDKLEGL KENIMLGNLI PAGTGLTGIE EVMEIAEEYH KNEY
