RPOB_MARN8
ID RPOB_MARN8 Reviewed; 1358 AA.
AC A1TYJ0;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Maqu_0712;
OS Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter
OS aquaeolei).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=351348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700491 / DSM 11845 / VT8;
RX PubMed=21335390; DOI=10.1128/aem.01866-10;
RA Singer E., Webb E.A., Nelson W.C., Heidelberg J.F., Ivanova N., Pati A.,
RA Edwards K.J.;
RT "Genomic potential of Marinobacter aquaeolei, a biogeochemical
RT 'opportunitroph'.";
RL Appl. Environ. Microbiol. 77:2763-2771(2011).
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; CP000514; ABM17809.1; -; Genomic_DNA.
DR RefSeq; WP_011784241.1; NC_008740.1.
DR AlphaFoldDB; A1TYJ0; -.
DR SMR; A1TYJ0; -.
DR STRING; 351348.Maqu_0712; -.
DR PRIDE; A1TYJ0; -.
DR EnsemblBacteria; ABM17809; ABM17809; Maqu_0712.
DR KEGG; maq:Maqu_0712; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000000998; 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; 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..1358
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300344"
FT REGION 1033..1053
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1358 AA; 151419 MW; 0402BA694E166024 CRC64;
MTYSYTEKKR IRKDFSKLPS VMEVPYLLSI QLDSFRDYLQ METAPEDRRE TGLHAAFKSV
FPIVSYSGNA ALEYVSYRIG EPVFDVKECQ LRGVTYAAPL RVKVRLIIYD KESSNKAIKD
IKEQEVYMGE MPLMTENGTF VVNGTERVIV SQLHRSPGVF FDHDKGKTHS SGKLLYSARV
IPYRGSWLDF EFDPKDAVFV RIDRRRKLPA SILLRGLGYT SEQMLEMFFE TSKFSLGAEV
CKLELVPSRL RGDIATFDIK DNDGNVIVEE GRRITARHIK QLEKAGITEL EVPTEYLYGR
VLAKDMIDQS TGEVLVECNT ELTEEVVTKI LDAGVKDIET LYTNDLDCGP FMSDTLRIDP
TRTPLEALVE IYRMMRPGEP PTKESAENLF NNLFFSEERY DLSAVGRMKL NRRLGREEST
GEGTLTHDDI IDVLKTLIAI RNGQGQVDDI DNLGNRRVRC VGEMAENQFR VGLVRVERAV
RERLSLAESE GLMPQDLINA KPVAAAVKEF FGSSQLSQFM DQNNPLSEVT HKRRISALGP
GGLTRERAGF EVRDVHPTHY GRVCPIETPE GPNIGLINSL ATYARSNSYG FLESPYRKVV
DGVVTDEVVY LSAIEESNYV IAQASAATDE GKRLTDELVT VRHQNEFTVA PPEAVNFMDV
SPRQVVSVAA SLIPFLEHDD ANRALMGANM QRQAVPTLKS QVPLVGTGVE RTVAQDSGVC
VTARRGGVIE SVDAARIVVR VNNEETEAGD AGVDIYNLTK YTRSNQNTCI NQRSIVRQGD
VIARGDVLAD GPSVDLGELA LGQNMRIAFM PWNGYNFEDS ILISEKVVQE DRLTTIHIQE
LTCVARDTKL GSEEITADIP NVGESALSKL DESGIVYIGA EVGPGDILVG KVTPKGETQL
TPEEKLLRAI FGEKASDVKD TSQRVPTGTR GTVIDVQVFT RDGIEKDARA LSIEKEQLDK
YRKDLKDEYR IVEGATFERL MAALKGQEVI SGPGLKKGAK LEEAYLAELP RADWFKLRMK
DEALNELLEK SEQGLEDRKK EHEARFDDKK GKLQQGDDLA PGVLKIVKVY LAIKRRIQPG
DKMAGRHGNK GVISAVMPIE DMPYDEFGNT VDIVLNPLGV PSRMNVGQVL ETHLGAAAKG
LGERISRMLD EQRKVAELRK LLDEIYNHSD EVFKVDLDSL TDKEIFELCN NLRGGVPMAT
PVFDGAKEAE VKRMLELAGL DTTGQTKLYD GRTGDAFDRP VTVGYMYILK LNHLIDDKMH
ARSTGSYSLV TQQPLGGKAQ FGGQRFGEME VWALEAYGAA YTLQEMLTVK SDDVNGRTKM
YKNIVDGDHR MEPGMPESFN VLVKEIRSLG IDIELESE
