RPOC_MYCPN
ID RPOC_MYCPN Reviewed; 1290 AA.
AC P75271;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=MPN_515;
GN ORFNames=MP327;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00089; AAB95975.1; -; Genomic_DNA.
DR PIR; S73653; S73653.
DR RefSeq; NP_110203.1; NC_000912.1.
DR RefSeq; WP_010874871.1; NC_000912.1.
DR AlphaFoldDB; P75271; -.
DR SMR; P75271; -.
DR IntAct; P75271; 14.
DR STRING; 272634.MPN_515; -.
DR EnsemblBacteria; AAB95975; AAB95975; MPN_515.
DR KEGG; mpn:MPN_515; -.
DR PATRIC; fig|272634.6.peg.569; -.
DR HOGENOM; CLU_000524_3_0_14; -.
DR OMA; YRNIRVE; -.
DR BioCyc; MPNE272634:G1GJ3-845-MON; -.
DR Proteomes; UP000000808; 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; 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..1290
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067763"
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 530
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 532
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 534
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 909
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 985
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 992
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 995
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1290 AA; 144895 MW; 0A52BC2D70EA5146 CRC64;
MTKRNKKNNK LYKNIKAIKL SIASNDTILN WSEGEVTKAE TINYKSLKPE PGGLFDEAIF
GPVKDYECAC GKFKKIKYRG VRCDRCGVWV TESIVRRERM GHIALVSPVA HIWMSKELPS
PSKISLVLNI SYKEVEQVLY FVNYIVLDTG KIKDPKIMPF KFKEVLDLAG KGSLTTRQKM
RRVIGYIFRN LIKNRSSEDY RKGKIFYESL KNSSLPFSLN DAFNYIKKYT GFRVGIGAEA
ILELLNKIDL NYEFSKLNDA LRKAKKDSVE DAKVKKILRQ LETISWFRNS KLHPKNMILH
TVPVIPPDIR PIIQLDGAKF TTSDINNFYR RVIIRNDRLR RILEDGTVPA IVVNNEKRLL
QESVDALFDN SSRHKPALSK DKRSLKSLTD RLKGKQGLFR HNLLGKRVDY SGRSVIVVGP
ELKMYEVGIP ALMILKLFKP FIIHGLINKF DSNGNEIRPI ASSIRQAEDM IKNQDDLIWG
IVYDVIKDRP VLLNRAPTLH RLGIQAFEPR IVDGKAIRLH PLVTTAFNAD FDGDQMAVHV
PLSENAVNEA RAILLASKHI LGLKDGRPIV TPTQDMVLGN YYLTTERKGQ TGEGIIFGTV
HEARAAYEAG KVHLHAIVGI STKAFPNKHF EAQGTLITTV GKIIFNDVLG DNIPYINEGE
FDEHACPQKF IVPPSGDVRA AIAAHQVLPA FGKKVISKLI DLLYTVVEFK DLPRILENIK
ALGFKYSTHS STTVSVFDIP KYSNKQQYFD EADQQVLKYK QFYNKGLLTD DERYKRVVKL
WNGVKEKVSS EIQDLIKREE YRDNSIVVMA DSGARGNISN FTQLFGMRGL MSKSFNYERN
NQSKIIKDTI EVPIKHSFLE GLTINEYFNS SYGARKGMTD TAMKTAKSGY MTRKLVDATH
ELIINHDDCG TRKGIVVEAI VETKTRSLVE SLFDRIVNRY TIGPILDPET KAEIVPANSL
ITQELAKQIC ATSIKQVLVR SVIYCERENG VCQYCFGVDL STGKLVELGT AVGVIAAQSI
GEPGTQLTMR TFHTGGVSTE NNLAQGFERL KQIFEVVAPK DYERCVISEV KGVVKSITTT
QNAQEVLIES SVDERTYSIP FSAQLRVKVG DAVELGSKIT EGSIDIRQLL RVAGIQRVRQ
YMIVEIQKVY RIQGIEIADK YVEIIIRQLT SLLQVTDAGS SNLFVGQLVH SHHLNELNKS
LLLSGKMPVI AINQVFGIDE AASKSNSFLS AASFQDTKKI LTDAAVKTQV DYLLGLKENV
IIGGKIPAGT GFLTDEELAY LGAKTVQEEY
