RPOB_CERSK
ID RPOB_CERSK Reviewed; 1377 AA.
AC B9KL83;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=RSKD131_0006;
OS Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=557760;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KD131 / KCTC 12085;
RX PubMed=19028901; DOI=10.1128/jb.01565-08;
RA Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL J. Bacteriol. 191:1118-1119(2009).
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; CP001150; ACL99865.1; -; Genomic_DNA.
DR RefSeq; WP_002722478.1; NC_011963.1.
DR AlphaFoldDB; B9KL83; -.
DR SMR; B9KL83; -.
DR EnsemblBacteria; ACL99865; ACL99865; RSKD131_0006.
DR GeneID; 57469046; -.
DR GeneID; 67445492; -.
DR KEGG; rsk:RSKD131_0006; -.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001597; Chromosome 1.
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; Transcription;
KW Transferase.
FT CHAIN 1..1377
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165818"
SQ SEQUENCE 1377 AA; 153818 MW; 43FBB838B235C6F5 CRC64;
MAQSYVGQKR IRRYYGKIRE VLEMPNLIEV QKSSYDLFLK SGDGPKAADG EGIQGVFQSV
FPIKDFNETA VLEFVKYELE KPKYDVDECQ QRDMTYAAPL KVTLRLIVFD VDETTGARSV
KDIKEQDVYM GDMPLMTANG TFIVNGTERV IVSQMHRSPG VFFDHDKGKT HSSGKLLFAC
RIIPYRGSWL DFEFDAKDIV FARIDRRRKL PVTTLLYALG MDQEGIMDAY YETVNFKHQK
NRGWVTRFFP ERVRGTRPTY DLVDAATGEV ILKAGEKATP RMVKKWIDEA QITELLVPFD
HIVGRYVAQD IINEETGEIW VEAGDELTME YDRDGEVKGG TLKLLLDQGI TDIPVLDIDN
VNVGPYIRNT MAADKNMGRD TALMDIYRVM RPGEPPTVEA ASNLFDTLFF DSERYDLSAV
GRVKMNMRLD LGKPDTQRTL DRDDIIACIK ALTELRDGKG EIDDIDHLGN RRVRSVGELM
ENQYRVGLLR MERAIKERMS SVEIDTIMPQ DLINAKPAAA AVREFFGSSQ LSQFMDQTNP
LSEVTHKRRL SALGPGGLTR ERAGFEVRDV HPTHYGRMCP IETPEGQNIG LINSLATFAR
VNKYGFIETP YRKVVEGAVT DDVVYMSATE EMRHTVAQAN AQLDEEGRFV SDLISSRKAG
EFMLNPPDAI DLIDVSPKQL VSVAASLIPF LENDDANRAL MGSNMQRQAV PLLQSDAPFV
GTGIEAVVAR DSGAAIMARR AGVIDQVDAT RIVVRATEML EPGEPGVDIY RLRKFKRSNQ
SSCINQRPLV KVGDVVHRGE VVADGPCTDM GELALGRNVI VAFMPWNGYN YEDSILISER
ILRDDVYTSI HIEEYEVAAR DTKLGPEEIT RDIPNVGEEA LRNLDEAGIV YIGAEVQPGD
ILVGKITPKG ESPMTPEEKL LRAIFGEKAS DVRDTSLRLP PGAYGTIVEV RVFNRHGVDK
DERALQIERE EVERLARDRD DELAILERNI YSRLRTLIMG KTAVKGPKGI RAGSEINEDL
LSTLSRGQWW QLALGEEADA KEVEALHEQF EAQKRALDHR FEDKVEKVRR GDDLPPGVMK
MVKVFVAVKR KLQPGDKMAG RHGNKGVISK VVPIEDMPFL ADGTHVDLVL NPLGVPSRMN
VGQILETHMG WAARGLGIKI DEALQDYRRS GDLTPVKEAM RLAYGDETYE GAFGDREDED
LVEMAGRVTK GVPIATPVFD GAKEPDVNDA LRRAGFDQSG QSIVFDGRTG EQFARPVTVG
VKYMLKLHHL VDDKLHARST GPYSLVTQQP LGGKAQFGGQ RLGEMEVWAL EAYGAAYTLQ
EMLTVKSDDV AGRTKMYESI VKGEDNFEAG VPESFNVLVK EVRGLGLNME LLDADEE
