RPOC_MALP2
ID RPOC_MALP2 Reviewed; 1288 AA.
AC Q8EWX0;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=MYPE800;
OS Malacoplasma penetrans (strain HF-2) (Mycoplasma penetrans).
OC Bacteria; Tenericutes; Mycoplasmoidales; Mycoplasmoidaceae; Malacoplasma.
OX NCBI_TaxID=272633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HF-2;
RX PubMed=12466555; DOI=10.1093/nar/gkf667;
RA Sasaki Y., Ishikawa J., Yamashita A., Oshima K., Kenri T., Furuya K.,
RA Yoshino C., Horino A., Shiba T., Sasaki T., Hattori M.;
RT "The complete genomic sequence of Mycoplasma penetrans, an intracellular
RT bacterial pathogen in humans.";
RL Nucleic Acids Res. 30:5293-5300(2002).
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; BA000026; BAC43870.1; -; Genomic_DNA.
DR RefSeq; WP_011076906.1; NC_004432.1.
DR AlphaFoldDB; Q8EWX0; -.
DR SMR; Q8EWX0; -.
DR STRING; 272633.26453538; -.
DR PRIDE; Q8EWX0; -.
DR EnsemblBacteria; BAC43870; BAC43870; BAC43870.
DR KEGG; mpe:MYPE800; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000002522; 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..1288
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067762"
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 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 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 522
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 524
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 526
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 903
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 979
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 986
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 989
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1288 AA; 145306 MW; 7DEC0ED39FC9DBF9 CRC64;
MNSKSSRITS IQIGLASPEK IREWSNGEVT KSETINYKSL KPEKDGLFDE AIFGPVKDYE
CACGKYKKIK FRGKICEKCG VEITESIVRR ERVGHIELAA PIAHIWMTKE LPCPSKISLV
LDISYKEIEQ VVYFVNYIVL DEGNGKFPKN FNFKEVIDLS SQKSSKETRS KLRKTLREIY
ESIDVEASME NAIKHKIART FYDTLAESNM PFSIEEVFNF ISSFTGMRFG IGAEAILELL
KNIDLDKEYK DIYEKLRKSE NTSDIKTKKL VRRLEAIKWL KDSNNKPEWM ILKNIVVTPP
DTRPIIQLEG GKFTTSDINS FYRKIIIRNE RLKRVIQNNA PSIILNNEKR LLQEAVDALF
DNASRKKPLL GKDKRPLKSL SEHLKGKQGL FRQNLLGKRV DYSGRSVIVI GPELKMYQVG
IPVSMILKLF KPFIIHELIK KTDDEGNTKD PIVSNIKSAE KLILNQDNTI WPIINKVIKQ
RPVLLNRAPT LHRLGIQAFE PILVEGKAIR LHPLVTTAFN ADFDGDQMAV HVPLSPEAVA
EARTIILASW HILGPKDGKP IITPTQDMVL GNYYLTMEKL NMPGQGMLFA NVDELKTVYQ
MKKVHVHSII GIPTSAFPKK QFPKDGILIT TVGKVILNDV LPEEMSYLNN PDNLEELSDN
DIVEWGKDYR TFIEKKKVYK AFTKKTLSEI VNILHRKYSD ASLEIVPSTM DKIKDIGFEY
STKSATTISA FDVPEYTEKE KYFEETDKKV EEMKKYYQKG LLTDDERYKK VVSAWSSVTN
QVSKDIEKLI QKPEYLTNSI VIMANSGARG NISNFTQLSG MRGLMSKSYN YDQKQKSKVI
KDTIEVPIKN SFIEGLTVSE YFNSSYGARK GMTDTAMKTS KSGYMTRKLV DATQDVIVNN
EDCKTKKGTI LEVIEDTKSG SVIESLNERL INRFPIFDVV HPKSKKVLAP AGEIITKAVA
NEIVDAGIDK VEVRSVLHCK EENGICQKCF GTDLTTNKLV EKYTAIGVIA AQSIGEPGTQ
LTMRTFHTGG VSSGTNIAQG FERLKQLFDI IPPKQWEKSI ISEIEGKVSS IKASPDNPNI
LVVTIKNSKE SINYKVPFDS ELRVEEGDKV KPGSKITEGS IDVKELLKVA GIEVVRNYII
KEVQKVYRLQ GIEIADKYIE VIIRQLTNKV QIQDSGNSDF FIGQIIDINT FRKENEKLIL
SDDKVPATAV NLIFGLDEAP SKTGSFLAAA SFQDTKKILT DACVKGQIDS LNGLKENVIF
GNLIPCGTGK KSNEDIIEEG NKMYELEY
