RPOC_MYCMO
ID RPOC_MYCMO Reviewed; 1424 AA.
AC Q6KI08;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=MMOB2820;
OS Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS mobile).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=267748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX PubMed=15289470; DOI=10.1101/gr.2674004;
RA Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA Church G.M.;
RT "The complete genome and proteome of Mycoplasma mobile.";
RL Genome Res. 14:1447-1461(2004).
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; AE017308; AAT27768.1; -; Genomic_DNA.
DR RefSeq; WP_011264802.1; NC_006908.1.
DR AlphaFoldDB; Q6KI08; -.
DR SMR; Q6KI08; -.
DR STRING; 267748.MMOB2820; -.
DR PRIDE; Q6KI08; -.
DR EnsemblBacteria; AAT27768; AAT27768; MMOB2820.
DR KEGG; mmo:MMOB2820; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR OrthoDB; 4421at2; -.
DR Proteomes; UP000009072; 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; 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..1424
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225552"
FT BINDING 552
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 554
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 556
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 1424 AA; 161754 MW; C85E868DE470DEC7 CRC64;
MNKILKGDNQ NWAEYEIDSI SLALATDEDV LNWSNGEVTK PETVNYKTYK PEKHGLFDEL
IFGPTTDYKC PICGKKYKIS NEGSTCGNTE ECKREKPEIL PKISRRSRMG HIRLHAPIVH
FWFFKVDNSI ISKLLGLKSE NSNKYYSKKE IEALIYYTSH IVVESGGLNS LPKHTVIYSD
NAAIIYRDAL EEIRSKYDRS IPEQNEIIEE ISEALVNLAE LKNANSSKKE NSKQEKDYGI
DFYEYNEIIE EYSGAKIKTG SEAVEYLLKN FDLTAEQEVI KDKIKALNEA IEKESKTSQS
KVEERKKLYK RLSIINAFIN SNQKPESMLI RNLPVIPADL RPLIQLDGGR HSTSDINELY
RRIIIRNNRL KKWQESNAPQ IIIQNELRMI QESVDALIDN QRRSPSPVVS KENRPLKSIS
DALTGKKGRF RQNLLGKRVD YSGRSVIVVG PDLKMHQAGI PRQMAAKLFE PWIIKELIEK
EIAPTIKSAK KLIEDQNPII WPHVARVIVD KPVLLNRAPT LHRLSIQAFE PVLIRGKAIK
LHPLVTTAFN ADFDGDQMAV HVPISDESVR EAKELLMANR NILGPKDGEP IINPSQDIIL
GLYYLTREVK GAKGEAKYYM SYDDMYAAYS SKKIDLHARV AIPYRTVKAF KVNQNVEYII
STVGKFIFNR AFPDNFPFIF DNKFDNYRNN EENKYLVPKG TKLDEYIKNL PVNNPFNKKE
IAKFVRIVFD EFSGAMPISK IASVVKKVNS GNYHDTVMMY ADLFKDKQNK KSVRHAQILA
NYTKQEFEKI NKKLTLQNEG VERVWDSKHR SELLEKIWFA YNNIVASVLD KIKVLGFKFS
MQSGSTFSIN DIKTSLDKEK YVKEGEEYIN NLNKMYENGF ITDDEKYTLA ISEWAKIKEK
ITNSLKKIIE DNKENSIFMM MQSGARGNIS NYVQLAGMRG LMANNVKTLK ADAQNERVVR
STVEVPVKSS FLDGLTAYEF YSSTHGARKG LTDVALNTAR SGYLTRRLVD VAQNIVVSED
DCGSDFGLKV KDITDTRTAT IIVPLIERIE GRYLNSALYS NEGQLLANKN TLVTEEFADQ
IVNKYNIKEV EIRSILGCHT RNGVCKLCYG KDLASNAPVN IGEAVGIIAA QSIGEPGTQL
TMRTFHTGGV AGVEDITGGF GRLIELIDAF EKPWGLLAQI SKWYGVVSEI KESKTASNKL
IVSIKEDFKN TLRTEEVSKD RKLRVKVGDR VKPGSKITEG PIVLKELLKY TDARTVQKYL
LKEIQRLYRM QGISISDKYI EIIIRQMLSK VDIVEPGDSN FFAGSIVDIF EYQEENGRLL
SEGKKPAYGK VIIKGAKQSP LLSDSFLAAA SFQETAKILV HSAISRKVDE LSGLKENIIL
GHKIPSGTSS KYEVDSKYDI RDPKSFFEDE SKYEYLKFED KWIA
