RPOB_SHEAM
ID RPOB_SHEAM Reviewed; 1342 AA.
AC A1S211;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-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=Sama_0206;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
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 Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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; CP000507; ABL98417.1; -; Genomic_DNA.
DR RefSeq; WP_011758328.1; NC_008700.1.
DR AlphaFoldDB; A1S211; -.
DR SMR; A1S211; -.
DR STRING; 326297.Sama_0206; -.
DR EnsemblBacteria; ABL98417; ABL98417; Sama_0206.
DR KEGG; saz:Sama_0206; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000009175; 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..1342
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300396"
SQ SEQUENCE 1342 AA; 150176 MW; 8FB678F764084F09 CRC64;
MVYSYSEKKR IRKDFGKRPQ VLDIPYLLSI QLDSFKKFTD QDPTGERGLE AAFRSVFPIK
SFSGNSELQY VSYKLGEPVF DVKECQIRGV TYSAPLRVKL RMVLFDREAA PGTVKDIKEQ
EVYMGDIPLM TENGTFVING TERVIVSQLH RSPGVFFDHD RGKTHSSGKV LYNARIIPYR
GSWLDFEFDP KDALFVRIDR RRKLPATIIL RALDFSTQDI LDIFFERVDF TIKKDSLVMK
LLPERLRGET ASYDIKDAEG NIVVEKGRRI TARHIRQLEK TNTTELEVPV EYIVGKIAAQ
DYIDPDTGEV LVTANNEIRL EDLAQLSLAG IKDISTLYIN ELDHGAYISD TLRIDSTTNR
LEALVEIYRM MRPGEPPTKD AAEALFQNLF FSEERYDLSK VGRMKFNRRL EIADDVGTGV
LSNDDIVAVM KKIIEIRNGN DEVDDIDHLG NRRIRSVGEM AENQFRVGLV RVERAVRERL
SLGDLNELMP QDLINAKPIS AAVKEFFGSS QLSQFMDQNN PLSEVTHKRR ISALGPGGLT
RERAGFEVRD VHPTHYGRLC PIETPEGPNI GLINSLATFA RTNSYGFLET PYRKVVDGVV
TDDVEYLSAI EEGRYVIAQA NIELDGEGRI LEEQVACRHK GESTFMRASD IQYMDVSPQQ
IISVAASLIP FLEHDDANRA LMGANMQRQA VPTLRSEKPL VGTGIERALA VDSGVVVAAK
RGGVIDYVDA SRIVVKVNED ELRPGEAGID IYNLTKYTRS NQNTCINQRP CCQVGDPIVR
GDVLADGPST DLGDLALGQN MRVAFMPWNG YNFEDSILIS ERVVQDDRFT TIHIQELSCI
ARDTKLGSEE ITADIPNVGE SALSKLDESG IVYIGAEVKG GDILVGKVTP KGETQLTPEE
KLLRAIFGEK ASDVKDSSLR VPNSVTGTVI DVQVFTRDGV EKDKRAIEIE EMHIAQARKD
LSEEFKILEE GVLSRARNLL LAGGYTQAQL DAIPRKELLT QVIDDETKQT ELEQLAEQHE
ELKADFDKKF EHKRRKITQG DDLAPGVLKI VKVYLAVKRT IQPGDKMAGR HGNKGVISKI
CPIEDMPYDE QGNPVDIVLN PLGVPSRMNI GQVLEVHMGA AAKGIGNRIQ AMLEEQREVA
ELRGYIKQAY DLGETQQKVD IESFTDEEVI RLAKHLKDGL PTATPAFDGA KEKEIKQMLE
LAGLPTSGQL RLFDGRTGNA FEREVTVGYM YMLKLNHLVD DKMHARSTGS YSLVTQQPLG
GKAQFGGQRF GEMEVWALEA YGAAYTLQEM LTVKSDDVNG RTQMYKNIVD GNHQMQPGMP
ESFNVLLKEI RSLGINIELD QE
