RPOB_THEM4
ID RPOB_THEM4 Reviewed; 1172 AA.
AC A6LKB8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=Tmel_0502;
OS Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429).
OC Bacteria; Thermotogae; Thermotogales; Fervidobacteriaceae; Thermosipho.
OX NCBI_TaxID=391009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12029 / CIP 104789 / BI429;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Detter J.C.,
RA Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermosipho melanesiensis BI429.";
RL Submitted (MAY-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; CP000716; ABR30369.1; -; Genomic_DNA.
DR RefSeq; WP_012056730.1; NC_009616.1.
DR AlphaFoldDB; A6LKB8; -.
DR SMR; A6LKB8; -.
DR STRING; 391009.Tmel_0502; -.
DR EnsemblBacteria; ABR30369; ABR30369; Tmel_0502.
DR KEGG; tme:Tmel_0502; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_0; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001110; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 2.
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_0000329193"
SQ SEQUENCE 1172 AA; 132745 MW; 8489422FEB1E0608 CRC64;
MKEIKRGKRT RYSFERVQTP IPVPNLVEIQ TKSYQDFLEN GILKVLKKFS PITSSKSDLR
KEKGFSLEFV SVRIGEPQNT VQECKERLLT YTVPVYTTVR ITDNSTNEMI EEEAFLGYIP
YMTPRTTFII NGAERVVVNQ LVRSPGIYFV EEAKKTSGTK PIYVAHFLPV RGAWLEILLN
LNDEVFYARI DRKRRINLFL LLKALGYSED LELLSLFPYW IDVEDEYTLQ HSEGLIILED
VKTKNGGLIA KRGDVITQGL IEKLENSDIQ KIKVAHRYAV NTLEKLNHVY GENIEENRAY
IEIFRKLRPG ELPRINAAKI FLRNLYFNEE RFELSEVGRF KMNNRLEEAY RKYLIEVEGK
DPQGVEEVKY DETSNVLTPM DIVLASRNLI EIDKHPGTMD TKDHLGNKRV RTVGELIRIE
FERAFSKAVF MIQEKLATYT SLDKISVQSL INVKSIIATI NSFFATNPLS QFMDQTNPLA
ELTHKRRLTA VGPGGLKRER ARFEVRDVHH SHYGRMCPIE TPEGANIGLI TSLSVYSSID
KFGFLITPYV KVVKGKVTNE IVYLTADEEE NYKIAPSTIP IDEKGNIIPE NVTVRYEEKV
LYVNKNNVQF IDVAPNQIVS VSTSLIPFLE HDDANRALMG SNMQRQGVPL IETEAPRVGT
GMEWEAAKYS GTLILAKHDG IVKKVDAQKI VIHRIDENGK EMYDSMGNPM LDIYELLKFT
RTNQDTCINQ RPIVNVGEIV KKDEPIADGP ATDMGELALG KNVLVAFVPW EGYNFEDAIL
ISEELLEKET YTSIHIEVYE TTARDTRLGP EEITPDIPNV SKEKLRNLDE DGIIRIGAYV
QETDILVGKV TPKSESDTTP EEKIIRSVFG EKGKEVKDTS LRVPHGIEGR VIAVHVFDKE
KDGDLGPGVN KLIRVYVAIR KPLEVGDKLA GRHGNKGVVS KILPKEDMPF LPDGTPIQVV
LSPLGVPSRM NVGQILETSL GWLAMLTNRW FATPVFDGAK EGDILPELYK ARKKFGLEMG
DFEENPSGKV ILRDGRTGKE FDHPILVGYM YVMKLIHIAR DKIHARSTGP YSLIHQQPLG
GKAQFGGQRF GEMEVWALEA YGAAHTLNEM LTVKSDDIRG RNEVYKAIMK GKNIPEPGLP
ESFKVLVREL RGIALDVRVY DDEGNEIDIE KL
