RPOB_MESFL
ID RPOB_MESFL Reviewed; 1284 AA.
AC Q6F0L7;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=Mfl598;
OS Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS (Acholeplasma florum).
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC Mesoplasma.
OX NCBI_TaxID=265311;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
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_01321}.
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_01321};
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_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; AE017263; AAT75956.1; -; Genomic_DNA.
DR RefSeq; WP_011183496.1; NC_006055.1.
DR RefSeq; YP_053840.1; NC_006055.1.
DR AlphaFoldDB; Q6F0L7; -.
DR SMR; Q6F0L7; -.
DR STRING; 265311.Mfl598; -.
DR EnsemblBacteria; AAT75956; AAT75956; Mfl598.
DR GeneID; 2897590; -.
DR KEGG; mfl:Mfl598; -.
DR PATRIC; fig|265311.5.peg.602; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_14; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000006647; 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:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1284
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224072"
SQ SEQUENCE 1284 AA; 142777 MW; BE2EDFB480BA0BF1 CRC64;
MAYKIKKVNR GVERRDYRKV SGNLELPNLI EIQTKTFEWF KTKGIDEVLN EFFAMSSNDA
SASLFLEGWE IKEAKISPSK AKEQSKIYDA PIYVDLQLMF TKTEDISKEF EEIVEKDVKK
VLSNWIAEKT DSKNVSLVKN TDNIYFFDVK LKGTEKNDLF QITILEEKED IIVAEVSVRK
WGQVFFGDFP LMTDAGTFVI NGSQKVIVSQ LVRSPGSYFK TEINNKTGES LYNGDIIPSR
GTWLEFETDT KKTAETTNSL FVKIDKSRKT TATSFLKILG LDRDTILNIY DKDKVIVETL
KNDNDTGDTY ADWAQHVQEI YKKIRQGETA TSDGASKYIN GLLFDRRKYD LTKAGRFKLQ
QKLAVKNRLM GRILAEDIVD ASGKILVAKN TEISKANIKE VSDALSQDGV MVSSIEYRED
IPGSRQIQKV KVYQDNNSKD ETFTIVGITP NSKEEHITVV DIVATVSYLL GLEYNIGEYD
DIDNLANRRV RTVGELLQNQ FRMGLTRIDK NVKEKLSTSD LYKVKVSTII NAKPLTAVIG
EFFNLSQLSQ FMDQINPLAE LTNKRRLTAL GPGGLSRDRA SLEVRDVHPS HYGRICPIET
PEGPNIGLIN NLSTYAIVDE LGFIRTPYLK VIDGVIQNEH EYLSADEEKE YIISQSNVTK
DENGKILDET VVSHYKGDDY IAKVSEVQFI DVSPKQIVSV ATSAIPFLEN DDANRALMGA
NMQRQAVPTI VPESPFVGTG IEFEAARDSG VCIVATENGI VKYVDAKQIT VESKAGIKTY
TLANFERSNN GSSIVQKPIV KVGDSIEAGQ IIADGPSVDN GELALGQNVV VAFTTYNGYN
FEDAIVMSER VIMEDKFTSV HIDEYVLEVR NTKQGAEEIT SEIPNISDNA KKYLDNEGIV
AIGTEVKTGD ILVGKVTPKG QTQLSPEDKL LHAIFGEKSR SVKDNSLKVP NGGEGIVQSV
KRFKAKSAAN PDGIDLPADV LEVIKVYIVQ KRKIQEGDKM SGRHGNKGII SKVLPVEDMP
HLEDGTPVDI LLNPQGIPSR MNIGQILEIH LGMAAKKLGV KIATPVFEGV NSNDLDEIMA
EAGMENYGKV KLIDGQTGEA IDKPISVGVM YMLKLSHMVD DKLHARSVGP YSLITQQPLG
GKAQNGGQRF GEMEVWALEA YGAAHTLREI LTIKSDDLKG RTKTYEAIVR SKNIPTPGTP
ESFNVLSKEI MGLGFDIYLL DNKGNKSQIN AYDDDNDLIN DESMKHASID KLTFEDSISL
VEIEDLDSFE EVDESEINLS FEEE
