RPOC_MYCPU
ID RPOC_MYCPU Reviewed; 1426 AA.
AC Q98Q24;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, 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=MYPU_5450;
OS Mycoplasmopsis pulmonis (strain UAB CTIP) (Mycoplasma pulmonis).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=272635;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAB CTIP;
RX PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C., Blanchard A.;
RT "The complete genome sequence of the murine respiratory pathogen Mycoplasma
RT pulmonis.";
RL Nucleic Acids Res. 29:2145-2153(2001).
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 1 Zn(2+) ion per subunit; 2 are expected compared to other
CC organisms. {ECO:0000305};
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}.
CC -!- CAUTION: The highly conserved N-terminal zinc-binding site of this
CC subunit is not present in this sequence. {ECO:0000305}.
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DR EMBL; AL445565; CAC13718.1; -; Genomic_DNA.
DR PIR; A99580; A99580.
DR RefSeq; WP_010925346.1; NC_002771.1.
DR AlphaFoldDB; Q98Q24; -.
DR SMR; Q98Q24; -.
DR STRING; 272635.MYPU_5450; -.
DR EnsemblBacteria; CAC13718; CAC13718; CAC13718.
DR KEGG; mpu:MYPU_5450; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; MPUL272635:G1GT6-553-MON; -.
DR Proteomes; UP000000528; 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; 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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1426
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067764"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 536
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 538
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1009
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1085
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1092
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1095
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1426 AA; 160697 MW; 656C4B64EAF6BE39 CRC64;
MPKTRKYSTV DEEKILKVSL SLATKEDVLE WSHGEVTKPE TINYKSYKPE RHGLFDELIF
GPATDYKCPI CGKKYKKSNE GLTCNNTPQC EIEKPEILPK ISRRSRMGHI ALQTPVVHFW
FFKIDNSIIS KLLVLRVGES NEYVSKNDLE NIIYYKSHIV LDNGGLKSLP KNKIININNA
AQIYKDALIE LRELNLNDAD ALEIIDGTIN HLNDIVGSKV GNDYGVDFYE LNEVIEEYSS
AKIQTGSKAI EFLLENIDLE EEQRKIKSKI KEINNLEKTS SSRKQDLSKL YKRLQVVESF
INSGQKPTSM LIYNLPVIPA ELRPLVQLDG GRHSTSDINE LYRRIIIRNN RLRKWIELNA
PTLITQNELR MIQEAVDALI DNSKKKPKPV TSKDNRNLKS ISDALTGKKG RFRQNLLGKR
VDYSGRSVIV VGPELKMNQV GIPREMAAKL FEPWIIKELI DQEITLSVKS ARKLIDNLNP
IIWPHVAKVI QGRPVLLNRA PTLHRLSIQA FEPVLIRGKA IKLHPLVTTA FNADFDGDQM
AVHVPISDEA VREAKELLFA NRNILGPKDG EPIINPSQDM ILGIYYLTIE IAGAKGEAKV
FQDVNSMLRA YEEGSVSLHA RVAIPFKKLQ KTFNLKGDKG YIFSTVGKFI FNQAFPENFP
FIFDSSVSSI SDAQEYTKKY YIPYGLNIKE TIQNTPINDA LSKKDLSKII RTIFDKYVPV
LTKEDVASVI NDVNHTNYKD TSTKFANLVT TNKTALEYIH AESLSKFTTK HFVDVNKKLS
LKTPGNPNQP IWEVDQYVEL LENVWFDYVN IVASVLDEIK DLGFKFSTKS GTSISIHDIE
VSDNKKERIK EGDDYTSELK SMYREGLLTD DERYSLTINK WSEVKDNIQN DLKKIVKNNP
LNPIFIMMNS GARSNMANYV QLAGIRGLMT NNTKILKSDA ENERVVRSTV EIPVKSSFLD
GLTAYEFYSS THGARKGLTD TALNTAKSGY LTRRLVDVAQ GIVVTEKDCA TQNGFVVKDI
VDNKTKTVIV PIRERIEGRF TIEDVKDKDG NVIVEKDTLI DAKMAEEIVE VHDVKEVNIR
SILGCEAKNG VCQKCFGKDL ATSRIVSIGE AVGITASQSI GEPGTQLTMR TFHSGGVAGV
EDITGGFGRL TELIDAYRSP WGRPAIISKV DGIITEIKTP KDKNTNLVYI TYLDQDDASQ
TEVVSVPKNR TLRVKVGDKI VKGQKIIDGP IILEELLEYG GPRKVQSYLL KEIQKIYRMQ
GIAINDKYIE IIISQMLSKI EISEPGDSDF IIGSLVNNLD FYNTNNELLE KGLEPAKGKV
VIHGAKRIPL LSNSFLAAAS YQESAKILVN SSISSQQDFL VGVKENIILG KKIPAGTNSQ
YESKSKFDIR DPKEYFKDKS PQRHYKIEMD NEVSDMFNEF RISQNK
