RPOC_META1
ID RPOC_META1 Reviewed; 1464 AA.
AC B3PM77;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=MARTH_orf213;
OS Metamycoplasma arthritidis (strain 158L3-1) (Mycoplasma arthritidis).
OC Bacteria; Tenericutes; Mycoplasmoidales; Metamycoplasmataceae;
OC Metamycoplasma.
OX NCBI_TaxID=243272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=158L3-1;
RX PubMed=18573899; DOI=10.1128/iai.00516-08;
RA Dybvig K., Zuhua C., Lao P., Jordan D.S., French C.T., Tu A.H.,
RA Loraine A.E.;
RT "Genome of Mycoplasma arthritidis.";
RL Infect. Immun. 76:4000-4008(2008).
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; CP001047; ACF07129.1; -; Genomic_DNA.
DR RefSeq; WP_012498086.1; NC_011025.1.
DR AlphaFoldDB; B3PM77; -.
DR SMR; B3PM77; -.
DR STRING; 243272.MARTH_orf213; -.
DR PRIDE; B3PM77; -.
DR EnsemblBacteria; ACF07129; ACF07129; MARTH_orf213.
DR KEGG; mat:MARTH_orf213; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000008812; 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.
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..1464
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000353395"
FT REGION 1435..1464
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1440..1464
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 541
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 543
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 545
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1022
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1098
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1108
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1464 AA; 165333 MW; 15CC23ADF8B9799B CRC64;
MKKSRKYATL DSDKIAKISL ALATPDDVES WSHGEVTKPE TINYKSYKPE RGGLFDEIIF
GPMIDYRCPI CGHKYKKINE GSFCSKTELC KQEKVEILPK ISRRNHMGHI KLNSPVVHFW
FFKVDHSIIF KLLDLTVAGR PNTEPVRRID LENLIYYKSH IVLESGGIKA LPKNLIIDIN
VAAVIYKDAL EELITRFEPG TEDYEDIRET LDNLIEKASS KIGQDYGIDF YELNEVIEHY
SEAKIGTGAQ AIEYLLKNLD LQKEKELVSA KIKKINDEEI MSGAKIASTS RQTREKLYKR
LQVINAFIES KQEPTSMLIY NLPVIPADLR PLIQLDGGRH STSDINELYR RVIIRNNRLK
QWQEKDAPTL VIQNELRMIQ EAVDALIDNA RRSPNPVLSK DNRPFKSISD ALTGKKGRFR
QNLLGKRVDY SGRSVIVVGP NLKMHQCGIP REMAAKLFEP WIIHRLIEKE VATTIKNAKK
MLEDQNPVIW PHIAEVIKGR LVLLNRAPTL HRLSIQAFEP VLVRGKAIRL HPLVCTPFNA
DFDGDQMAVH VPISERALLE SRELMLANKN ILGTKDGEPI INPSQDMILG IYYLTIEEPG
ALGEGRIFDN YEHMIRAYEA KKVSLHARVA LPIEEVKNSK IKAFASRESQ RYIISTVGKF
IFNNIFPKSF PFIFDNKVTE ATSLEQYSEK VNKYIIPAGT NVIEHIKMEL PVLDAFNKKN
IAKIIRYVFD KYVAALTLQD VAGVIDQLND VPLSNIVLNY LNLKTYDDRK VDQEHAIILA
ALTRSATEKT KARSQRHIEG LEVPLNAEEK AEILDDVWFR YTNMVASILD DIKDLGFKYS
SLSGITFAIS DILETDKKPE YIAEGDAYIA QLKQYYNDGL ISDDDRYSLT IKKWTDIKAK
VQGELQQIIK ENPRNPIITM INSGARGNIS NYVQLAGMRG LMANNTKSTR ADVKNERVVR
STVEIPVKSS FIEGLTAFEF YSSTHGTRKG ATDTALNTAK SGYLTRRLVD VAQNIVVRKE
NCGSDYGHIV RDIVDTKNGQ IIVPLKERII GRYANKPIIG EKTKQELAKR NTLITDKLAQ
KIIDEGVKEV EIRSVLGCNT KNGVCKMCFG KDLATNRVVN IGEAVGIIAA QSIGEPGTQL
TMRVFHTGGV AGAEDITGGF PRLIELIDAH EQPWGRPAVI SPYEGEIVED LVEDKNVNSH
LLTIKVVNSK KETVNKKVHV YTTKKLRVKV GDHVKVGQKL SEGPVIVKEL LELTDTITVQ
NYLLKEIQKI YRIQGIAISD KYIEIIIRQM MSKIVIHDPG DSKFFAGAIV DIFDYQEENA
TLLSQRKRPA FGKVVIKGAK QVPLLSDSFL AAASYQETSK ILVHAAISSR SDSLSGLKEN
IIVGKKIPAG TALYPFESHS KYDIRPSIDY FRKPELETSD SEFIPVDLES YHQELEDEQQ
QIIEVDDSDI SVEDEENDFY ENED
