RPOB_MYCSJ
ID RPOB_MYCSJ Reviewed; 1172 AA.
AC A3PV78;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-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_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=Mjls_0997;
OS Mycobacterium sp. (strain JLS).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; unclassified Mycobacterium.
OX NCBI_TaxID=164757;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JLS;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA Sims R.C., Richardson P.;
RT "Complete sequence of Mycobacterium sp. JLS.";
RL Submitted (FEB-2007) 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; CP000580; ABN96805.1; -; Genomic_DNA.
DR AlphaFoldDB; A3PV78; -.
DR SMR; A3PV78; -.
DR STRING; 164757.Mjls_0997; -.
DR KEGG; mjl:Mjls_0997; -.
DR HOGENOM; CLU_000524_4_3_11; -.
DR OMA; FMTWEGY; -.
DR BioCyc; MSP164757:G1G8C-1009-MON; -.
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; 1.
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; Transcription;
KW Transferase.
FT CHAIN 1..1172
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300350"
SQ SEQUENCE 1172 AA; 129079 MW; F84A0673C6D63D81 CRC64;
MLEGCILAVS SQSKSAKAIT NNSVPGAPNR ISFAKLREPL EVPGLLDVQT ESFDWLIGAD
SWRQRATARG DVNPTGGLEE VLTELSPIED FSGSMSLSFS DPRFDEVKAP VDECKDKDMT
YAAPLFVTAE FINNNTGEIK SQTVFMGDFP MMTEKGTFII NGTERVVVSQ LVRSPGVYFD
ESIDKSTEKT LHSVKVIPGR GAWLEFDVDK RDTVGVRIDR KRRQPVTVLL KALGWTNEQI
TERFGFSEIM MSTLEKDNTA GTDEALLDIY RKLRPGEPPT KESAQTLLEN LFFKEKRYDL
ARVGRYKVNK KLGLNTDKPI TSSTLTEEDV VATIEYLVRL HEGQATMTVP GGVEVPVEVD
DIDHFGNRRL RTVGELIQNQ IRVGLSRMER VVRERMTTQD VEAITPQTLI NIRPVVAAIK
EFFGTSQLSQ FMDQNNPLSG LTHKRRLSAL GPGGLSRERA GLEVRDVHSS HYGRMCPIET
PEGPNIGLIG SLSVYARVNP FGFIETPYRK VENGVVTDQI DYLTADEEDR HVVAQANSPL
DDEGHFTEDR VLVRRKGGEV EFVSATEVDY MDVSPRQMVS VATAMIPFLE HDDANRALMG
ANMQRQAVPL VRSEAPLVGT GMELRAAIDA GDVVVSEKAG VVEEVSADYI TVMADDGTRH
TYRMRKFARS NHGTCANQRP IVDAGQRVEA GQVVADGPCT QNGEMALGKN LLVAIMPWEG
HNYEDAIILS NRLVEEDVLT SIHIEEHEID ARDTKLGAEE ITRDIPNVSD EVLADLDERG
IVRIGAEVRD GDILVGKVTP KGETELTPEE RLLRAIFGEK AREVRDTSLK VPHGESGKVI
GIRVFSREDD DELPAGVNEL VRVYVAQKRK ISDGDKLAGR HGNKGVIGKI LPVEDMPFLP
DGTPVDIILN THGVPRRMNI GQILETHLGW VAKAGWNINV AGADGVPDWA EKLPEELYSA
PSDSIVATPV FDGARENELS GLLASTLPNR DGDVMVNEDG KAELFDGRSG EPFPYPVTVG
YMYILKLHHL VDDKIHARST GPYSMITQQP LGGKAQFGGQ RFGEMECWAM QAYGAAYTLQ
ELLTIKSDDT VGRVKVYEAI VKGENIPEPG IPESFKVLLK ELQSLCLNVE VLSSDGAAIE
MRDGDDEDLE RAAANLGINL SRNESASVED LA