RPOB_GLUOX
ID RPOB_GLUOX Reviewed; 1390 AA.
AC Q5FTX7;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
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=GOX0386;
OS Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconobacter.
OX NCBI_TaxID=290633;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=621H;
RX PubMed=15665824; DOI=10.1038/nbt1062;
RA Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT oxydans.";
RL Nat. Biotechnol. 23:195-200(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAW60169.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000009; AAW60169.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041242769.1; NC_006677.1.
DR AlphaFoldDB; Q5FTX7; -.
DR SMR; Q5FTX7; -.
DR STRING; 290633.GOX0386; -.
DR PRIDE; Q5FTX7; -.
DR EnsemblBacteria; AAW60169; AAW60169; GOX0386.
DR KEGG; gox:GOX0386; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR Proteomes; UP000006375; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1390
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224061"
SQ SEQUENCE 1390 AA; 155016 MW; B63A8B8D69FD5F7A CRC64;
MNAITKSFTG RKRIRKSFGR IPEIAPMPNL IDVQRASYEA FLQMNVSPDS RQDAGLQEVF
RSVFPINDFA GRGRLDFMSY EFEDPKYDVE ECIQRGLTYA APLKVILRLT TWDIDEDTGS
RSIHDMKEQP VYMGDMPLMT DNGTFIINGT ERVIVSQMHR SPGVFFDHDK GKTHSSGKYL
FAARVIPYRG SWLDFEFDAK DLIYVRIDRK RKLPVTTLLY ALEGANYLAQ REQKIAEGGD
VEGLDIRGMD QDEILSYFYE AVPFTRLGGE WARPFDPDAF RGLKLLSPLV DADTGEVVAE
ADAKLTARMV RKIAEKTRVV QVGRLDILGR FLAYDLVNEN TGEIYGEAGE ELTEDRLAAL
EEMGITELPL LSVDGSHGPW IRNTLAADKN SCRDEALIDI YRIMRPGEPP TKETAEAMFH
GLFFDQGRYD LSAVGRVKMN MRLDVDAPDT LRVLRKEDIL RTIKIMCELK DGRGQIDDID
NLGNRRVRSV GELMENQYRV GLLRMERAIR ERMGSVDIDT VMPHDLINAK PAAAAVREFF
GSSQLSQFMD QTNPLSEVTH KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETAGR
PNIGLINSLS TYAKVNKYGF IETPYRLVEE GVLQDGWKYL SAMEEEKLVV AQADAKQDDQ
GRLTDELVSV RRSGDFRVVP PDQVTACDVS PKQLVSVAAA LIPFLENDDA NRALMGANMQ
RQAVPLVKAD APLVGTGMEA AVAHDSGATI VAKRRGVIDQ IDGARIVVRA TDEAGATQGV
DIYRLRKYMR SNQSTCINQR PLVKVGDTVH AGDIIADGPS TELGELALGR NVLVAFMPWN
GYNFEDSILI SERIARDDVF TSIHIEEFEV MARDTKLGQE EITRDIPNVG EEALRNLDEA
GIVYVGAEVN PGDILVGKVT PKGESPMTPE EKLLRAIFGE KASDVRDTSL KLPPGTTGTI
VDVRVFSRRG VDKDERAMAI ERAEIERLTK DRDDERGIQE RSFYNRLRER LIGQTAGAGF
KGIRSGTPIT EEVLDEHHRA TWASITVTSD EVMAELEKLR GEFKEATRRI DARFDSKVEK
LQRGDELPPG VMKMVKVFVA VKRKLQPGDK MAGRHGNKGV VSRVVPVEDM PFLENGQAVD
IVLNPLGVPS RMNIGQILET HLGWACANIG ASIGDMVDEY QRTGERKQEL LDRLHEVYGD
VIFNEDVATL PNEQLIELAN NLRKGLPIAT PVFDGASIPD IEEMLEKAGV NKSGQSQLID
GRTGEPFERQ TTVGYIYMLK LHHLVDDKIH ARSIGPYSLV TQQPLGGKAQ FGGQRFGEME
VWALEAYGAA YTLQEMLTVK SDDVSGRTKV YEAIVREQDD FEAGIPESFN VLIKELKSLG
LNVELEQSGL
