RPOC_MYCGA
ID RPOC_MYCGA Reviewed; 1286 AA.
AC P47716;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 122.
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=MYCGA2140;
GN ORFNames=MGA_1005;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-13.
RC STRAIN=A5969Var.B;
RX PubMed=8714123;
RA Skamrov A.V., Rozovskaia T.A., Gol'dman M.A., Feotistova E.S.,
RA Bibilashvili R.S.;
RT "Determination of the nucleotide sequence of the part of the Mycoplasma
RT gallisepticum genome, containing the rpoB gene, during the use of the Bal-
RT pTM method for obtaining sequential deletions of the sequenced fragment.";
RL Mol. Biol. (Mosk.) 30:61-75(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}.
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DR EMBL; AE015450; AAP56564.1; -; Genomic_DNA.
DR EMBL; L38402; AAB40952.1; -; Genomic_DNA.
DR RefSeq; WP_011113455.1; NC_004829.2.
DR AlphaFoldDB; P47716; -.
DR SMR; P47716; -.
DR GeneID; 57203528; -.
DR KEGG; mga:MGA_1005; -.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000001418; 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..1286
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067758"
FT BINDING 66
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
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 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 527
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 529
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 531
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 905
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 981
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 988
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 991
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1286 AA; 145059 MW; FB8C242C2D4AC693 CRC64;
MDKLNKKNKN KRIRGLQISI ASAEEMRSWS HGEVKKPETI NYKSLKPETD GLFDEAIFGP
VKDFECACGK YKKIKHRGRT CEKCGVEITE SIVRRERMGH IDLAVPVAHI WMTKELPSPS
KISLVLDVSY KEVEEVVYFV NYIILNPGNS KNPVFKFKEV VDLSGKGSKS ARIKLRKVLR
EIKDKHQADK HSIIYKRASD YYNKLKESHL PFSIDEVAKF IETHTGIRLG IGAEAILELL
EGVDLQKEYD LINEELNSYS KDLKANKEDQ KVKRALRRLE TIKWLKESGI KASNMILKVI
PVTPPDTRPI IQLDGARFTT SDINNFYRRI IIRNERLKKI IELRAPSVIL NNEKRMLQEV
VDALFDNASR KKPITAKDKR PLKSLTDRLK GKQGLFRQNL LGKRVDYSGR SVIVIGPELK
MYEVGIPAPM ILKLFKPFII RELIMRFNED GQEIKPIAPN IKIAEQMIAQ KSERIWDIVD
KVIKERPVLL NRAPTLHRLG IQAFEPKIVD GKAIRLHPLV TTAFNADFDG DQMAVHVPIS
KEAVAEARAI MLASWHILGP KDGKPVATPT QDMVLGNYYL TTEKRNEKGE GLIFSDFDQV
ILAYEAKQVS IHALIGLSTK CLTKKPFAKQ GIVITTVGKA IMNSIMPEEM AYLNDGDNLL
ELDESNIVFA GEDFKQKLAK RPLYKPFGKK TLSKIIEILY KNFPLQKVPQ VLDKIKEFGF
KYSTLSSTTI SVFDIPRYDN KQEYITKANE MIAKLKHMYQ KGLLTDDERY TKVIRLWADV
KDNVSRDIKE IITRPEYKEN SIVVIADSGA RGNISNFTQL FGMRGLMSKS YNYDQKIKSQ
VIRDTIEVPI KHSFIEGLTI NEYFNSSYGA RKGMTDIAMK TSKSGYMTRK LVDAAQEVII
NDSDCNTNKG IVVSTITNSL DGGVVETLSE RIVTRYTIDP IYDEKTKELL VDADTLITSE
LAEKIAKANV TKALIRSPIY CQSTKGLCQK CFGNDLTTND LVQIGTAIGV IAAQSIGEPG
TQLTMRTFHT GGTANEGNIT QGFERLKQIF DVVSPKEWEL ATIAENEGVV ESITSDATAR
IIRIKTRLEA EEYRVPFDAV ISVNPKDVVY PGSKLTEGSI DIKHLLRVAG IETVRQYFLE
EVQKVYRLQG IEIADKYVEV TIRQLTNKLQ VIDVGDSDYF VGQTVDINKF RKEVTNMLIA
NKRPPVAINQ VFGLDEAPAK TGSFLSAASF QDTKKILTDA AVKNQIDYLV GLKENVILGN
LIPAGTGFMS SEEIIKAGEE ALEKEY
