RPOC_MYCGE
ID RPOC_MYCGE Reviewed; 1292 AA.
AC P47582; Q49292; Q49454; Q49483; Q49486;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 31-JAN-2018, sequence version 2.
DT 03-AUG-2022, entry version 135.
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=MG340;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-142 AND 1029-1148.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 334-506.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=1945886; DOI=10.1093/nar/19.21.6027;
RA Peterson S.N., Schramm N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A random sequencing approach for placing markers on the physical map of
RT Mycoplasma genitalium.";
RL Nucleic Acids Res. 19:6027-6031(1991).
RN [4]
RP SEQUENCE REVISION TO 818, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=16407165; DOI=10.1073/pnas.0510013103;
RA Glass J.I., Assad-Garcia N., Alperovich N., Yooseph S., Lewis M.R.,
RA Maruf M., Hutchison C.A. III, Smith H.O., Venter J.C.;
RT "Essential genes of a minimal bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:425-430(2006).
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 -!- DISRUPTION PHENOTYPE: Probably essential, it was not disrupted in a
CC global transposon mutagenesis study. {ECO:0000269|PubMed:16407165}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01322}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA43746.1; Type=Frameshift; Evidence={ECO:0000305};
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; L43967; AAC71565.2; -; Genomic_DNA.
DR EMBL; U01797; AAD12323.1; -; Genomic_DNA.
DR EMBL; U02169; AAD12451.1; -; Genomic_DNA.
DR EMBL; X61528; CAB98132.1; -; Genomic_DNA.
DR EMBL; X61534; CAA43746.1; ALT_FRAME; Genomic_DNA.
DR PIR; F64237; F64237.
DR RefSeq; WP_010869441.1; NC_000908.2.
DR AlphaFoldDB; P47582; -.
DR SMR; P47582; -.
DR STRING; 243273.MG_340; -.
DR EnsemblBacteria; AAC71565; AAC71565; MG_340.
DR KEGG; mge:MG_340; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR BioCyc; MGEN243273:G1GJ2-427-MON; -.
DR Proteomes; UP000000807; 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..1292
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000067759"
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 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 85
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
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 536
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 911
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 987
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 994
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 997
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT CONFLICT 33..36
FT /note="WSEG -> LIWR (in Ref. 2; AAD12323)"
FT /evidence="ECO:0000305"
FT CONFLICT 338..344
FT /note="NDRLRRI -> KWPIKKD (in Ref. 3; CAA43746)"
FT /evidence="ECO:0000305"
FT CONFLICT 1029..1037
FT /note="LTMRTFHTG -> MDNAYFPYW (in Ref. 2; AAD12451)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1292 AA; 145705 MW; AF5939913B87DF4D CRC64;
MTTTRRNKRN NKLYKNIKAI KLSIASNDTI LNWSEGEVTK AETINYKSLK PEPGGLFDEA
IFGPVKDYEC ACGKFKKIKY RGVRCDRCGV WVTESIVRRE RMGHIALVSP VAHIWMSKEL
PSPSKISLVL NISYKEVEQV LYFVNYIVLD TGKIKDDKIM PFKFKEVLDL TGKGSLSTRQ
KMRRVIGYIF RNLIKSKSSE DYRKGKIFYE SLKNSSLPFS LNDAFNYIKK YTGFRVGIGA
EAILELLNKI DLNLEFSRLN DALRKAKKDS VEDAKVKKIL RQLETISWFR NSKLHPKNMI
LHTVPVIPPD IRPIIQLDGA KFTTSDINNF YRRVIIRNDR LRRILEDGTV PSIVVNNEKR
LLQESVDALF DNSSRHKPSL SKDKRSLKSL TDRLKGKQGL FRHNLLGKRV DYSGRSVIVV
GPELKMYEVG IPALMILKLF KPFIIHGLIN KFDENGNEIR PIAASIRQAE DMIKNQDDLI
WGIVYDVIKD RPVLLNRAPT LHRLGIQAFE PRIVDGKAIR LHPLVTTAFN ADFDGDQMAV
HVPLSENAVN EARAVLLASK HILGLKDGRP IVTPTQDMVL GNYYLTTERK GQLGEGIIFS
TVYEARAAYE SQKVHLHAIV GISTKAFPNK KFACQGTLIT TVGKIIFNDV LGNNVPYIND
GEFDENACPE KFIVKQGEDV RQSILKHQII PAFSKKVISK LIDLLYLLLE FKDLPKTLDN
IKALGFKYST FSSTTVSVFD IPKYTNKQNY FDSADQQVLK YKQFYNKGLL TDDERYKRVV
KLWNNVKEKV SDEIQNLIKQ EQYRDNSIVV MADSGARCNI SNFTQLFGMR GLMSKSFNYE
RNNQSKIIKD TIEVPIKHSF FEGLTINEYF NSSYGARKGM TDTAMKTAKS GYMTRKLVDA
THELIINHDD CGTRKGIVVE AIVETKTKSL IESLFDRIVN RYSITPIVDP ETQKTIVEAN
SLITTQLAKQ ICATSIKEVL VRSVIYCERE NGICQYCFGI DLSTGKLVEL GTAVGVIAAQ
SIGEPGTQLT MRTFHTGGVS TENNLAQGFE RLKQIFEVVT PKDFEKAVIS EVKGTVKSIT
TVQNAQEVVI KSNVDERIYT IPFSAQIRVH VGDQVSPGSK ITEGSVDIKQ LLRIAGIQRV
RQYMIVEIQK VYRIQGIDIA DKYVEIIIRQ LTNLLQVTDA GNSNLFVGQL VHSHYLNELN
KSLLLAGKMP VIAINQVFGI DEAASKSNSF LSAASFQDTK KILTDAAVKN QVDYLLGLKE
NVIIGGKIPA GTGFLTDEEL TFLGSKTVAE EY
