RPOB_PELUB
ID RPOB_PELUB Reviewed; 1363 AA.
AC Q4FLL2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=SAR11_1123;
OS Pelagibacter ubique (strain HTCC1062).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Pelagibacterales;
OC Pelagibacteraceae; Candidatus Pelagibacter.
OX NCBI_TaxID=335992;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC1062;
RX PubMed=16109880; DOI=10.1126/science.1114057;
RA Giovannoni S.J., Tripp H.J., Givan S., Podar M., Vergin K.L., Baptista D.,
RA Bibbs L., Eads J., Richardson T.H., Noordewier M., Rappe M.S., Short J.M.,
RA Carrington J.C., Mathur E.J.;
RT "Genome streamlining in a cosmopolitan oceanic bacterium.";
RL Science 309:1242-1245(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; CP000084; AAZ21926.1; -; Genomic_DNA.
DR RefSeq; WP_011282159.1; NC_007205.1.
DR AlphaFoldDB; Q4FLL2; -.
DR SMR; Q4FLL2; -.
DR STRING; 335992.SAR11_1123; -.
DR PRIDE; Q4FLL2; -.
DR EnsemblBacteria; AAZ21926; AAZ21926; SAR11_1123.
DR GeneID; 66295612; -.
DR KEGG; pub:SAR11_1123; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_5; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002528; 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..1363
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224088"
SQ SEQUENCE 1363 AA; 152478 MW; EB0F1F97A6447AC5 CRC64;
MQLSFTQKKN VRKSFGKLAE TLSIPNLIEV QKNSYKQLTD FDSEAGDLSK GFDRVFKSIF
PIEDLNDKAT LEYVSYRLEK PKFDTEECIQ RGLSFTSALK CTLRLVVYEI DQENNTKDIL
SAKEQEVYMG EVPMMTDSGT FITNGVQRVV VNQMHRSPGV FFDHDKGKSH ASGKLLFNCR
VIPNRGSWLD LEYDVKDFLY FKIDRKKKIF ASTLLMALGL TKSEIADEFY DKDTYSFDAK
TGKWKTKFNP ENYKAKNFSE EVTDAKTGNV VIKLGDKINF LTAKKLASDG LKDILVSQES
LIGKYLHNEV KVSDDEEEGT FGIGTELNDT IIKQILEANI SSIEISITNS INKGPYLLTT
ILNDKNNSKN DAITEIYKVL RPGEPPTVEI ATQIFNNLFF SSDRYDLSDV GRVKMNSRLN
LECSDKITIL RNDDIIAIVH KMLDLRDGKD EVDDIDHLGN RRVRSVGELV ENQARIGVYR
MERAIKEKMT TLDIESAMPQ DLINAKPLTV SLKDFFVSSQ LSQFMDQTNP LSEITHKRRV
SALGPGGLTR ERAGFEVRDV HPTHYGRICP IETPEGPNIG LINSLSTYAK INKYGFIESP
YKKVLNGIVQ DKVEYLSAME ETKYTIAQAN AKIDKSGKIL EELVPCRENL NFVLSNPSKI
DYIDVSPKQL VSVAASLIPF LENDDANRAL MGSNMMRQAV PLLKPESPLV GTGIESDVAL
DSGVTIVASR DGTVDKIDGK RIVIKATEET DFTKSGVDIY NLQKFKRSNQ NTCINQKPLV
RVGDKVKSGD IIADGPSTKL GELALGKNVT VAFMPWQGYN FEDSILISER CVTDDVFTSV
HIVEYEVMAR DTKLGEEEIT RDIPNVNEEA LKNLDESGIV YIGAEVKAGD ILVGKVTPKG
DSASGPEEKL LRSIFGEKAI DVTDTSLKMS RGSSGTVVDV RVFNRHGIEK DERSITIERA
EIDTVQQDKI VEEEILERSI KQRANQILSG ASLTKKIKDL DEGTKLDLEI INKININDVF
KITVGNVNDE ASIAQLKDQY NQAKQDIQER FEDKVLKIRS GDDLLPSVMK MVKVFVAIKR
RLRPGDKMSG RHGNKGVVSK IVPVEDMPYR EDGRPVDIVL NPLGVPSRMN VGQILETHLG
WACKEFGEEV KRLVNENNKK FEKTEKISSF LKSVYGKEVF DGGIEKLNKT EFSDLCENLQ
NGIAISTPVF DGAKEKDVSE MLELAKLPTS GQTNLWDGRT GEMFDRPVTV GIIYMLKLHH
LVEDKIHARS TGPYSLVTQQ PLGGKAQLGG QRFGEMEVWA LEAYGASYTL QEILTVKSDD
VAGRVKVYET IVKGEENFES GIPESFNVLV KEIKSLALNI ELN
