RPOB_SHEB8
ID RPOB_SHEB8 Reviewed; 1343 AA.
AC A6WHS1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 77.
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};
GN OrderedLocusNames=Shew185_0189;
OS Shewanella baltica (strain OS185).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
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., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-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; CP000753; ABS06360.1; -; Genomic_DNA.
DR RefSeq; WP_006083607.1; NC_009665.1.
DR AlphaFoldDB; A6WHS1; -.
DR SMR; A6WHS1; -.
DR GeneID; 11770553; -.
DR KEGG; sbm:Shew185_0189; -.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
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; 2.40.270.10; -; 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; 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; Transcription;
KW Transferase.
FT CHAIN 1..1343
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000051981"
SQ SEQUENCE 1343 AA; 150034 MW; 3C42F63EF99ACC57 CRC64;
MVYSYSEKKR IRKDFGKRPK VLDIPYLLSI QLDSFKKFTD QDPTGERGLE AAFRSVFPIK
SFSGNSELQY VSYKLGEPVF DVKECQIRGV TYSAPLRVKL RMVLYDREAA AGTVKDIKEQ
EVYMGDIPLM TDNGTFVING TERVIVSQLH RSPGVFFDHD RGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDALFVRIDR RRKLPATIML RALEYSTQEI LDLFFERVEF KIKKDTLVMA
LVPERLRGET ASYDIKDAEG SVLVEAGRRI TARHIRQLEK TNTTELEVPV EYIVGKYAAQ
DYIDPDTGEV LVSANSEISL EDLAKLSLAG IKELSTLYIN ELDHGAYISD TLRIDSTTNR
LEALVEIYRM MRPGEPPTKD AAEALFQNLF FSEERYDLSK VGRMKFNRRL SIPDDEGSGV
LSKEDIVAVM KNIIHIRNGF DEVDDIDHLG NRRIRSVGEM AENQFRVGLV RVERAVRERL
SLGDLNELMP QDLINAKPIS AAVKEFFGSS QLSQFMDQNN PLSEVTHKRR ISALGPGGLT
RERAGFEVRD VHPTHYGRLC PIETPEGPNI GLINSLASFA RTNSYGFLET PYRKVIDGVI
TDEVEYLSAI EEGRYVIAQA NIEIDANGRM AEEQIACRHK GESTFMRAAD IQYMDVSPQQ
IISVAASLIP FLEHDDANRA LMGANMQRQA VPTLRSEKPL VGTGIERTLA VDSGVVVVAK
RGGFVDYVDA SRIVVKVNED ELRPGEAGID IYNLTKYTRS NQNTCINQRP CCSVGEPVVR
GDVLADGPST DLGDLALGQN MRIAFMPWNG YNFEDSILIS ERVAQEDRFT TIHIQELSCI
ARDTKLGSEE ITADIPNVGE SALSKLDESG IVYIGAEVKG GDILVGKVTP KGETQLTPEE
KLLRAIFGEK ASDVKDSSLR VPNSVKGTII DVQVFTRDGV EKDKRAVEIE EMHIAQARKD
LGEEFKILEE GVLSRARNLL IGAGFTDAQI AALPRKDVLI QVIDDETKQT ELEQLAEQHE
ELKADFDKKF EIKRRKITQG DDLAPGVLKI VKVYLAVKRT IQPGDKMAGR HGNKGVISKI
CPIEDMPYDE QGNPVDIVLN PLGVPSRMNI GQVLEVHMGA AAKGIGNKIT AMLEEQRELA
EVRGYIKQVY ELGDEVQQRV DIDSFTDDEV LRLATNLKGG IPIATPAFDG AKEKEIKQML
ELAGLPTSGQ LKLFDGRTGN EFERQVTVGY MYMLKLNHLV DDKMHARSTG SYSLVTQQPL
GGKAQFGGQR FGEMEVWALE AYGAAYTLQE MLTVKSDDVN GRTQMYKNIV DGNHQMQPGM
PESFNVLLKE IRSLGINIEL DQA
