RPOB_MAGSA
ID RPOB_MAGSA Reviewed; 1391 AA.
AC Q2W2I1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=amb3140;
OS Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=342108;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AMB-1 / ATCC 700264;
RX PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT "Complete genome sequence of the facultative anaerobic magnetotactic
RT bacterium Magnetospirillum sp. strain AMB-1.";
RL DNA Res. 12:157-166(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}.
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DR EMBL; AP007255; BAE51944.1; -; Genomic_DNA.
DR RefSeq; WP_011385506.1; NC_007626.1.
DR AlphaFoldDB; Q2W2I1; -.
DR SMR; Q2W2I1; -.
DR STRING; 342108.amb3140; -.
DR PRIDE; Q2W2I1; -.
DR EnsemblBacteria; BAE51944; BAE51944; amb3140.
DR KEGG; mag:amb3140; -.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000007058; 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; 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..1391
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000237303"
SQ SEQUENCE 1391 AA; 154339 MW; DDD9485A50895BB4 CRC64;
MAKSYTGRKR VRKSFGRIPT VAPMPNLIEV QKSSYDHFLQ MDTAPEQRGN VGLQEVFKSV
FPIKDFSERG TLEFVRYELE QPKYDVEECQ QRGMTFAAPL KVTLRLVVWD IDEDTGSRSI
RDIKEQDVYM GDMPLMTSNG TFVINGTERV IVSQMHRSPG VFFDHDKGKT HSSGKYLFAA
RVIPYRGSWL DFEFDAKDLV YVRIDRRRKL PVTTLLYALD GMNTAALRAQ RAAEGRGLEQ
SEIKGMTSEE ILSYFYGKVV YTRGPKGWKT PFDAERLKGV KLVSDLIDAK SGEKVADAGS
KMTPRLGKKL REAGLTDIVV FPEDMIGQYV AEDIINEQTG EIFTEAGDEL TANLVAELEK
AGISELPVLA IDHINVGPYM RNTLAIDKNS SREEALIDIY RVMRPGEPPT LETAEALFTG
LFFDSERYDL SAVGRVKMNS RLNTPEVADT VRVLRKEDIL GVIKVLVELK DGKGEIDDID
HLGNRRVRSV GELMENQYRV GLLRMERAIR ERMSSVDIDS VMPHDLINAK PAAAAVREFF
GSSQLSQFMD QTNPLSEITH KRRLSALGPG GLTRERAGFE VRDVHPTHYG RICPIETPEG
PNIGLINSLA TYARVNQYGF IEAPYRKVFD GRVTSDVVYL SAMEEGRYTV AQANSILDAD
GRFTEDLVSC RRAGDFVMVP PNEINMIDVS PKQLVSVAAA LIPFLENDDA NRALMGSNMQ
RQAVPLIRAE APLVGTGMEQ AVARDSGAAI TAKRTGVVDQ VDATRVVIRA TEETQASASG
VDIYNLLKFQ RSNQNTCITQ RPLVKVGDLI QKGDIIADGP STQLGELALG RNVLVAFMPW
NGYNFEDSIL ISERIVRDDV FTSIHIEEFE VMARDTKLGQ EEITRDIPNV GEEALKNLDE
AGIVYIGAEV KPGDILVGKV TPKGESPMTP EEKLLRAIFG EKASDVRDTS LRLPPGVSGT
IVEVRVFSRR GVEKDERALA IERAEIERLA KDRDDERHIL ERSFFARLKA LIIGKKVVSG
PKGIKAGTVL ADANMDELHP STWRNIAIDD DAVMADAEAL KRAFDQQVDK LQERFENKVE
KLQRGDELPP GVMKMVKVFV AVKRKLQPGD KMAGRHGNKG VISRIVPLED MPYLEDGQQV
DIVLNPLGVP SRMNVGQILE THLGWACAGL GQQIGGMLDK YKRNAATIID LKSKLKDVYG
DAIYEDEIAG LADNEITELA HNLTPGVPIA TPVFDGARES DIVAMLTKAG RSSSGQVTLV
DGRTGEPFDR KVTVGYIYML KLHHLVDDKI HARSIGPYSL VTQQPLGGKA QFGGQRFGEM
EVWALEAYGA AYTLQEMLTV KSDDVSGRTK VYEAIVRGDD TFEAGIPESF NVLVKELRSL
GLNVELTQRN Y
