RPOC_MYCAP
ID RPOC_MYCAP Reviewed; 1478 AA.
AC A5IZ52;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=MAG6110;
OS Mycoplasmopsis agalactiae (strain NCTC 10123 / CIP 59.7 / PG2) (Mycoplasma
OS agalactiae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=347257;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10123 / CIP 59.7 / PG2;
RX PubMed=17511520; DOI=10.1371/journal.pgen.0030075;
RA Sirand-Pugnet P., Lartigue C., Marenda M., Jacob D., Barre A., Barbe V.,
RA Schenowitz C., Mangenot S., Couloux A., Segurens B., de Daruvar A.,
RA Blanchard A., Citti C.;
RT "Being pathogenic, plastic, and sexual while living with a nearly minimal
RT bacterial genome.";
RL PLoS Genet. 3:744-758(2007).
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; CU179680; CAL59311.1; -; Genomic_DNA.
DR RefSeq; WP_011949768.1; NC_009497.1.
DR AlphaFoldDB; A5IZ52; -.
DR SMR; A5IZ52; -.
DR STRING; 347257.MAG6110; -.
DR EnsemblBacteria; CAL59311; CAL59311; MAG6110.
DR KEGG; maa:MAG6110; -.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000007065; 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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1478
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353394"
FT BINDING 535
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 537
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 539
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1034
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1478 AA; 167186 MW; 18311D48774F2BE4 CRC64;
MSSFNKKIAK DIKKIKISLA AQDDVKNWSC GEVTKPETIN YKSYKPERDG LFDELIFGPT
TDFKCPICGT KYKKSDENTI CEKTPMCQKY QPVILPKMVR RSRMGHIHLE NPVVHFWFFK
IDHSIISKLL GLRIANSNKT VSKGDLEKLI YYKSHIVLED GGLKKLQKNA IIDISDAAII
YADALEELKE RFEKDTEEYE IISEALAELE SYAVSQTGQD YGIDFYEYNE IIHEFSKAKI
STGSKAIEYL LENIDLKAEA EFIESEIEKI NQHFDNNPTA SIKAQERSKL YKRLAVVNAF
IHSGQDPKSM LIYDLPVIPA DLRPLVQLDG GRHSTSDVNE LYRRIIIRNN RLKKWEETDA
PMLIKQNEFR MIQEAVDALI DNSRKKPAPV TSKDNRPLKS ISDTLTRKKG RFRQNLLGKR
VDYSGRSVIV VGPELKMHQV GVPREMAAKL FEPWIIKELI NGDSHINSIK AGKKAIENLD
PIIWPYVEKA IEGKVVLLNR APTLHRLSIQ AYEPVLIRGK AIKLHPLSCT PFNADFDGDQ
MAIHVPISEE AVREARELML ASKNILGPKD GEPIINPAQD IILGLYYLTM EKAAAIDGDK
VVGEGKFFAT YDEMLLAYEN KLVSLHARIA LPISEINKKR LNYSPENKYI ISTVGKFIFN
RAFPESFEFI FGKHVEYVNK TDANGEVKLS EKEVVYTSNN KNQLEQFLLP YGQNFAEVIA
KMPLNLPLSK KDVAKIVRRV YDKYVAIVTK SDVASVINQI NANEINQIFD LCAELKDFNG
KPIDVNHVEI LEKIIVEEYK AISQEIIVRE RTEEPIWTVN DYTKLLEIVW FKYTNIVANV
LDNIKELGYK FSTISGTTIS ISDVITHQDT KSRIAEGDKY IELLKDYFDQ GLMTDDERYN
ATIAKWAAIK DDIEKDLKKL TKLYPDNSLF MMFNSGARGN SSNFVQLAGM RGLMNNNTKV
LKADAENERV VRSTVEIPVK SSFLNGLTAY EFYSSTHGAR KGLTDTALNT AKSGYLTRRL
VDVAQGITVR EDDCGTDYGF QVKDILDTKT NTVIEALYDR IEGRFTNKAI YDKNGKLIVD
ADELITPEIA TEIVENGIKK VEIRSVLSCY TPNGVCKKCY GKDLALNRVV NIGEAVGVIA
AQSIGEPGTQ LTMRTFHTGG VAGVEDITGG FGRLIELIDA YDSPWGRPAV IANYYGRITD
IKRVKEGSES VEYDVITQEY KTRDGKVNTV EYKTRAGRKI RVKINDKVTP GQKIVEGPIV
LNNLLRVGDT RLVQNYILKE VQKLYRLQGI TISDKYIEII IRQMLSKILI TDSGDSDFFN
GSLVDIHVYQ KESARLISEG KKPPFGEVKI KGAKQIPLLS DSFLAAASYQ ETPKILVNAS
IKAQVDRLKG LKENIILGHK IPAGTNSNFE ENGKYDLRNP KSYFADKYDP DIKTVKFVAD
ENEILNMEHR VEIQHIFDEF QSEAFNANVI EFTDDSDN
