RPOC_MYCS5
ID RPOC_MYCS5 Reviewed; 1492 AA.
AC Q4A5S8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=MS53_0484;
OS Mycoplasmopsis synoviae (strain 53) (Mycoplasma synoviae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX NCBI_TaxID=262723;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=53;
RX PubMed=16077101; DOI=10.1128/jb.187.16.5568-5577.2005;
RA Vasconcelos A.T.R., Ferreira H.B., Bizarro C.V., Bonatto S.L.,
RA Carvalho M.O., Pinto P.M., Almeida D.F., Almeida L.G.P., Almeida R.,
RA Alves-Junior L., Assuncao E.N., Azevedo V.A.C., Bogo M.R., Brigido M.M.,
RA Brocchi M., Burity H.A., Camargo A.A., Camargo S.S., Carepo M.S.,
RA Carraro D.M., de Mattos Cascardo J.C., Castro L.A., Cavalcanti G.,
RA Chemale G., Collevatti R.G., Cunha C.W., Dallagiovanna B., Dambros B.P.,
RA Dellagostin O.A., Falcao C., Fantinatti-Garboggini F., Felipe M.S.S.,
RA Fiorentin L., Franco G.R., Freitas N.S.A., Frias D., Grangeiro T.B.,
RA Grisard E.C., Guimaraes C.T., Hungria M., Jardim S.N., Krieger M.A.,
RA Laurino J.P., Lima L.F.A., Lopes M.I., Loreto E.L.S., Madeira H.M.F.,
RA Manfio G.P., Maranhao A.Q., Martinkovics C.T., Medeiros S.R.B.,
RA Moreira M.A.M., Neiva M., Ramalho-Neto C.E., Nicolas M.F., Oliveira S.C.,
RA Paixao R.F.C., Pedrosa F.O., Pena S.D.J., Pereira M., Pereira-Ferrari L.,
RA Piffer I., Pinto L.S., Potrich D.P., Salim A.C.M., Santos F.R., Schmitt R.,
RA Schneider M.P.C., Schrank A., Schrank I.S., Schuck A.F., Seuanez H.N.,
RA Silva D.W., Silva R., Silva S.C., Soares C.M.A., Souza K.R.L., Souza R.C.,
RA Staats C.C., Steffens M.B.R., Teixeira S.M.R., Urmenyi T.P.,
RA Vainstein M.H., Zuccherato L.W., Simpson A.J.G., Zaha A.;
RT "Swine and poultry pathogens: the complete genome sequences of two strains
RT of Mycoplasma hyopneumoniae and a strain of Mycoplasma synoviae.";
RL J. Bacteriol. 187:5568-5577(2005).
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}.
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; AE017245; AAZ43893.1; -; Genomic_DNA.
DR RefSeq; WP_011283622.1; NC_007294.1.
DR AlphaFoldDB; Q4A5S8; -.
DR SMR; Q4A5S8; -.
DR STRING; 262723.MS53_0484; -.
DR PRIDE; Q4A5S8; -.
DR EnsemblBacteria; AAZ43893; AAZ43893; MS53_0484.
DR KEGG; msy:MS53_0484; -.
DR eggNOG; COG0086; Bacteria.
DR HOGENOM; CLU_000524_3_1_14; -.
DR OMA; YRNIRVE; -.
DR Proteomes; UP000000549; 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.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Magnesium; Metal-binding;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase;
KW Zinc.
FT CHAIN 1..1492
FT /note="DNA-directed RNA polymerase subunit beta'"
FT /id="PRO_0000225554"
FT REGION 1473..1492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1477..1492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 1032
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1114
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
FT BINDING 1117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01322"
SQ SEQUENCE 1492 AA; 169481 MW; 63A69FBBE206F686 CRC64;
MSNTFSKNNV KKIKQISLSL ATNEDVLSWS NGVVSKPETI NYKTYKPEKD GLFDEIIFGP
VTDFKCPICF TKYKKSDENT ICKRTTSCEK IQPKILPKIS RRSRMGHIAL NNPVVHFWFF
KINHSTISKL LGLKVAGSNK PVTKSDLEKI IYYKSHIVLE TGGLKSLQKN TIIDINDAAD
IYAGALEEIL EFNKDNKDGY EEILDTLNDL KEYAASKTGQ DYGIDFYEYN EIIEEYSQAK
IGTGSKAIEY LLKNIDLEKE SKEIQDEIDT INDQNKYEIS SSEALKRNKL YKRLAIIKSF
LKSGQKPENL LIYNLPVIPA DLRPLVQLDG GRHSTSDINE LYRRIIIRNN RLEKWYESDA
PVLIKQNEFR MLQEAVDALI DNSRKKPGPV TSKDGHPFKS ISDALVGKKG RFRQNLLGKR
VDYSGRSVIV VGPHLKMYQV GIPRDMAAKL FEPWIINRIM KEEEGINSVK AAKKLVDSLN
PIIWPYVEQV LENRPVLLNR APTLHRLSIQ AFQPVLIRGK AIKIHPLVTT AFNADFDGDQ
MAVHVPISKA AVREAQELML ASKNILGPKD GEPIINPSQD IILGLYYLTI EKANQKNEGK
FYPSFNEMML AYENKYINLA TRVVLPVSAL KKISILQKTD APYIYSTVGK FILNNAFPRD
FDFVFGKRVT EKLTSTNEHG EEVVSLKTKI DTSEHDIKRY VFNYGDNFTA KIKEADVNLP
LNKKEIAKIV RNIYEKYVPI VNIEDISQVI NKIDKTQLDN LHELCSELKD FNGNKLEDNR
IHLELLVRLI KEEFLKIQDQ YFAKDEESIF NHKYWELKHY TKLLERVWFR YSNYVSTVLD
VIKDLGFKFS TKSGITISMN DIVTSKTTKE RIKKAEEETE ALKDYFKKGY LTDDERYTLT
IKKWSDVKES IEKELKKVVD SNLDNPLFMM LSSGARGTYS NFTQLAGMRG LMNNNTKILK
ADAENDRVVR SIVEIPVKSS FLDGLTAYEF YSSTHGARKG LTDTALNTAK SGYLTRRLVE
VAQGVVIREE DCGSDYGFVV KDIKDTKTNT IIESLQERIE GRFTAVPIYD QNGKLIVKES
ELITPEIASE IVAKGITKVE IRSVLSCHTR NGLCKKCYGK DLATNRIVNI GEAVGVIAAQ
SIGEPGTQLT MRTFHTGGVA GGEDITGGFG RLIELIDAYD QPWGTPAEIS RHYGKVKKIE
TQKNKKGKES GQFNISVEYF DEDGNKQTHQ YLVKSSQRLR VKQGDEVVAG QKLSEGPIVL
NELLESVDTR AVQNYILKEV QKLYRLQGIA IADKYIEIII RQMLSKISII DPGDSSFYSG
SLVDAFVYQK ENGILLSQGK KPAYGVVKIK GAKQTPLLSD SWLAAASYQE TAKILVDASI
AKRTDNLEGL KENIIIGYKI PAGTNSNFEE NGKYNLKEFS SYFPNKYDST PELKLEEITD
ENIEEEFDYL KENTISEEEF ENLDDDTMYH LETSDEFEDE SFGEDDFEYS EE
