RPOB_TERTT
ID RPOB_TERTT Reviewed; 1360 AA.
AC C5BQ39;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 70.
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=TERTU_0883;
OS Teredinibacter turnerae (strain ATCC 39867 / T7901).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Teredinibacter.
OX NCBI_TaxID=377629;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39867 / T7901;
RX PubMed=19568419; DOI=10.1371/journal.pone.0006085;
RA Yang J.C., Madupu R., Durkin A.S., Ekborg N.A., Pedamallu C.S.,
RA Hostetler J.B., Radune D., Toms B.S., Henrissat B., Coutinho P.M.,
RA Schwarz S., Field L., Trindade-Silva A.E., Soares C.A.G., Elshahawi S.,
RA Hanora A., Schmidt E.W., Haygood M.G., Posfai J., Benner J., Madinger C.,
RA Nove J., Anton B., Chaudhary K., Foster J., Holman A., Kumar S.,
RA Lessard P.A., Luyten Y.A., Slatko B., Wood N., Wu B., Teplitski M.,
RA Mougous J.D., Ward N., Eisen J.A., Badger J.H., Distel D.L.;
RT "The complete genome of Teredinibacter turnerae T7901: an intracellular
RT endosymbiont of marine wood-boring bivalves (shipworms).";
RL PLoS ONE 4:E6085-E6085(2009).
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; CP001614; ACR14281.1; -; Genomic_DNA.
DR RefSeq; WP_015820397.1; NC_012997.1.
DR AlphaFoldDB; C5BQ39; -.
DR SMR; C5BQ39; -.
DR STRING; 377629.TERTU_0883; -.
DR PRIDE; C5BQ39; -.
DR EnsemblBacteria; ACR14281; ACR14281; TERTU_0883.
DR KEGG; ttu:TERTU_0883; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000009080; 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 Gene3D; 3.90.1110.10; -; 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; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1360
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000214489"
SQ SEQUENCE 1360 AA; 151313 MW; E2ED8931CA36CC49 CRC64;
MAYSYTEKKR IRKDFGKLPN VMEVPYLLAI QLDSYRKFTQ ADRPADERLD IGLQAAFKSV
FPIVSYSGNA ALEYVSYALG KPVFDVSECV LRGATYAVPL RVKVRLIIYD RESSSKAIKD
IKEQEVYMGE IPLMTDNGTF VINGTERVIV SQLHRSPGVF FEHDKGKTHS SGKLLYSARV
IPYRGSWLDF EFDPKDLVYV RIDRRRKLPA TILLRALGYS AEEMLDMFFE TSRVFLAEDN
IKLELVPSRL RGEVTTFEIK DADGNVIVED GRRITARHIR QLEKSNVTEL QVPAEYVLGK
ALANNVIDTN TGEVLFECNS EITEEVLEGL RSANVSEFQI LYTNDLDCGP FLSDTLRTDP
TRTELEALVE IYRMMRPGEP PTKESAEGLF QNLFFSNERY DLSAVGRMKF NRRLGRDEET
GEGTLSREDI VDVLRTLISI RNGQGTVDDI DHLGNRRVRS VGEMAENQFR VGLVRVERAV
KERLSMAESE GLMPQDLINA KPVAAAVKEF FGSSQLSQFM DQNNPLSEIT HKRRVSALGP
GGLTRERAGF EVRDVHPTHY GRVCPIETPE GPNIGLINSL ATYARTNNYG FLESPHRKVV
DGKVTDEIEY LSAINESQYV IAQASAATDG EGRLTDDLVS VRYQNEFTLK AAADVQYMDV
SPRQVVSVAA SLIPFLEHDD ANRALMGSNM QRQAVPTLKA DKPVVGTGME RNVARDSGVC
VVAKRGGKIE SVDAGRIVVR VADEETPAGD AGVDIYNLIK YTRSNQNTCI NQRPIVGPGD
SISRGDILAD GPSVDLGELA LGQNMRIAFM TWNGYNFEDS ILVSERVVQE DRFTTIHIQE
LTCIARDTKL GSEEITADIP NVGEGALAKL DESGIVYVGA EVGAGDILVG KVTPKGETQL
TPEEKLLRAI FGEKASDVKD TSLRVPSSVK GTVIDVQVFT RDGLEKDQRS LDIEKAQLDQ
VRKDLNEEYR IVEGATFARL RSSLVGNLAS SGKGVKKGEA VTDEMLNAID RDDWFKVRMA
DDALNEQLDL AEQQLVERRK ELDERFEDKK RKLATGDDLA PGVLKIVKVY LAIKRRIQPG
DKMAGRHGNK GVISVIMPVE DMPYDENGEP IDIVLNPLGV PSRMNVGQIL ETHLGLASKG
LGRKIDNMVK QQREIAELRK FLGEIYNEIG QGYKIEDLDS FSDEEILELA RNLRGGVPMA
TRAFDGAAES EIKALLKLAD LPESGQMSLF DGRTGDAFMR PVTVGYMYML KLNHLVDDKM
HARSTGSYSL VTQQPLGGKA QFGGQRFGEM EVWALEAYGA AYTLQEMLTV KSDDVNGRTK
MYKNIVDGDH RMEPGMPESF NVLVKEIRSL GINIELEQDS
