RPOB_GRAFK
ID RPOB_GRAFK Reviewed; 1270 AA.
AC A0M3Y9;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=GFO_2370;
OS Gramella forsetii (strain KT0803).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gramella.
OX NCBI_TaxID=411154;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT0803;
RX PubMed=17107561; DOI=10.1111/j.1462-2920.2006.01152.x;
RA Bauer M., Kube M., Teeling H., Richter M., Lombardot T., Allers E.,
RA Wuerdemann C.A., Quast C., Kuhl H., Knaust F., Woebken D., Bischof K.,
RA Mussmann M., Choudhuri J.V., Meyer F., Reinhardt R., Amann R.I.,
RA Gloeckner F.O.;
RT "Whole genome analysis of the marine Bacteroidetes'Gramella forsetii'
RT reveals adaptations to degradation of polymeric organic matter.";
RL Environ. Microbiol. 8:2201-2213(2006).
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; CU207366; CAL67334.1; -; Genomic_DNA.
DR RefSeq; WP_011710237.1; NC_008571.1.
DR AlphaFoldDB; A0M3Y9; -.
DR SMR; A0M3Y9; -.
DR STRING; 411154.GFO_2370; -.
DR PRIDE; A0M3Y9; -.
DR EnsemblBacteria; CAL67334; CAL67334; GFO_2370.
DR KEGG; gfo:GFO_2370; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_10; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000755; 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; -; 3.
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; 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..1270
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300322"
SQ SEQUENCE 1270 AA; 142739 MW; C8F986E1972EA5CF CRC64;
MLAKQTERLS FSSVKNKPAY PDFLDLQIKS FQDFFQLETK SEERGNEGLY NTFLENFPIT
DTRNQFVLEF LDYFVDPPRY SIQECIERGL TYSVPLKARL KLYCTDPEHE DFETIVQDVY
LGTIPYMTPS GTFCINGAER VVVSQLHRSP GVFFGQSFHA NGTKLYSARV IPFKGSWIEF
ATDINSVMYA YIDRKKKLPV TTLFRAIGFE RDKDILEIFD LAEEVKVSKT GLKKYLGRKL
AARVLNTWYE DFVDEDTGEV VSIERNEIVL DRDTELEKDH IEEILETGSK TILLHKEDNQ
TGDYAIIHNT LQKDPTNSEK EAVEHIYRQL RNAEPPDEET ARGIIDKLFF SDQRYSLGEV
GRYRMNKKLG LDVEMDKQVL TKLDIITIVK YLIELINSKA EIDDIDHLSN RRVRTVGEQL
SQQFGVGLAR MARTIRERMN VRDNEVFTPI DLINAKTLSS VINSFFGTNQ LSQFMDQTNP
LAEITHKRRL SALGPGGLSR ERAGFEVRDV HYTHYGRLCP IETPEGPNIG LISSLSVYAK
VNGMGFIETP YRSVTDGKIN TSEEPIYLSA EEEEGKKIAQ ANIPLKDDGT IDTDRVIARM
EGDFPVVDPK EIHYTDVAPN QISSISASLI PFLEHDDANR ALMGSNMMRQ AVPLLRTDSP
IVGTGLERQV ATDSRVLINA EGEGEVEYVD ANKIVIKYDR TEEERMVSFD DDSKSYNLIK
FRKTNQGSCI NLKPIISVGD RVTKGQVLCQ GYATEAGELA LGRNMKVAFM PWKGYNFEDA
IVISEKVVRD DIFTSIHIDE YSLEVRDTKL GNEELTNDIP NVSEEATKDL DEHGMIRVGA
EVKPGDILIG KITPKGESDP TPEEKLLRAI FGDKAGDVKD ASLKASPSLS GVVINKKLFA
RAIKDKRKRA QDKEDVAALE KKYDAKFANL KADLVEKLFT IIGGKTAQGV QNDLGEEVMP
KGKKYTLKML NAVDDYTHLT TGTWTTDDHL NELVADLLHN YKIKENDLQG NLRREKFTVS
VGDELPSGIL KLAKVYIAKK RKLKVGDKMA GRHGNKGIVA RIVRQEDMPF LEDGTPVDIV
LNPLGVPSRM NIGQIYETVL GWAGQKNGKK YATPIFDGAT IEEINDLTDK AGIPRYGHTY
LYDGGTGMRF DQRATVGVIY MLKLGHMIDD KMHARSIGPY SLITQQPLGG KAQFGGQRFG
EMEVWALEAY GASATLREIL TVKSDDVIGR AKTYEAIVKG EPMPEPGLPE SFNVLMHELK
GLGLDIKLEE
