RPOB_ACIF2
ID RPOB_ACIF2 Reviewed; 1362 AA.
AC B7J460;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-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}; OrderedLocusNames=AFE_0320;
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455;
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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; CP001219; ACK79513.1; -; Genomic_DNA.
DR RefSeq; WP_012536082.1; NC_011761.1.
DR AlphaFoldDB; B7J460; -.
DR SMR; B7J460; -.
DR STRING; 243159.AFE_0320; -.
DR PaxDb; B7J460; -.
DR PRIDE; B7J460; -.
DR EnsemblBacteria; ACK79513; ACK79513; AFE_0320.
DR GeneID; 66431376; -.
DR KEGG; afr:AFE_0320; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000001362; 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 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; 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..1362
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141652"
SQ SEQUENCE 1362 AA; 151762 MW; 3B84E808D646ADB5 CRC64;
MAYSFTEKKR IRKDFGKSQS ILAVPYLLAT QMDSYREFLQ ESVPPAARKE TGLEAVFRSV
FPMESYSGNA MLDYVSYRLE KPVFDVVECR QRGLTYCAGL RVRLRLAVME KDDTTGAKRV
KDVKEQDVYM GELPLMTEHG SFVINGTERV IVSQLHRSPG VFFDHDRGKT HSSGKLLFNA
RIIPYRGSWL DFEFDPKDHV YARIDRRRKL PATTLLRALG YSTQDILEMF FDMETFRLID
GDLRYVLIPQ RLQGEVAAFD IVSPETGDVL VQAGKRITVR QTKALSEVQG LHEIPVPDSF
LLGKVVARDI VHPETGEVVV QANEPVSGEL LDALRKMPSL TLHTLYLNEL DRGPYISETL
RIDTSRDAHD AQMEIYRLMR PGEPPTKDAA QNLFQGLFFS PDRYDLSAVG RMKFNRRVGR
DEITGPGVLN DADIIAVLKV LVALRNGVGE IDDIDHLGNR RVRSVGELME NQFRLGLVRV
ERAVKDRLAL AESEGLTPQD LINAKPIAAV VNEFFGSSQL SQFMDQTNPL SEVTHKRRVS
ALGPGGLTRE RAGFEVRDVH PTHYGRICPI ETPEGPNIGL INSLSCYART NSYGFLETPY
RRVVDRRTTD EVEYLSAIEE GNYMIAQANS TVDEHGVLTD ELVSCRFKNE FTLANPDQVQ
FMDISPRQIV SVAASMIPFL EHDDANRALM GSNMQRQAVP TVRSDAPMVG TGMERVVAID
SGAAVVARRG GVVDIVDGAR IVIRVSDEET LPEEPGVDIY NLVKYARSNQ NTTLNQRPVV
KVGDVVSRGD VLADGPSTEM GELALGQNIL VAFMPWNGYN FEDSILISER VVAEDRYTTI
HIEEFSVFAR DTKLGPEEIT RDIPNVAEGA LRHLDESGIV VIGAELAPGD ILVGKVTPKG
ETQLTPEEKL LRAIFGEKAS DVKDNSMRMP AGMYGTVIDV QVFTRDGIEK DARAKSIEEH
ELARIRKDLN DQYRIVEEDS YQRIERQLIG KVAEGGPNGL AAGNKVTKAY LKDLPRAKWF
EIRLRTEESN ESLEQIRAQL EEQRQRLDAV LEEKRRKLTQ GDDLSPGVLK MVKVHVAIKR
HLQPGDKMAG RHGNKGVVSK IVPVEDMPYL ADGTAVDIVL NPLGVPSRMN VGQILETHLG
WAAKGLGKKI GAMLDSEVAM AEMRAFLAEI YNRSGKKEDL DSLTDQEIRE LSANLRGGVP
MATPVFDGAS EEEIGDMLEL AGLPRSGQVT LYDGRSGDAF DRPVTVGYLY MLKLHHLVDD
KMHARSTGPY SLVTQQPLGG KAQFGGQRFG EMEVWALEAY GAAYTLQEML TVKSDDVSGR
SKMYESIVKG DFRMDAGMPE SFNVLLKELR SLGIDIELEQ SK
