RPOB_CHLAD
ID RPOB_CHLAD Reviewed; 1227 AA.
AC B8G4U9;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=Cagg_2707;
OS Chloroflexus aggregans (strain MD-66 / DSM 9485).
OC Bacteria; Chloroflexi; Chloroflexia; Chloroflexales; Chloroflexineae;
OC Chloroflexaceae; Chloroflexus.
OX NCBI_TaxID=326427;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-66 / DSM 9485;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Foster B., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Bryant D.A., Richardson P.;
RT "Complete sequence of Chloroflexus aggregans DSM 9485.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001337; ACL25575.1; -; Genomic_DNA.
DR RefSeq; WP_015941432.1; NC_011831.1.
DR AlphaFoldDB; B8G4U9; -.
DR SMR; B8G4U9; -.
DR STRING; 326427.Cagg_2707; -.
DR PRIDE; B8G4U9; -.
DR EnsemblBacteria; ACL25575; ACL25575; Cagg_2707.
DR KEGG; cag:Cagg_2707; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_0; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002508; 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; 2.40.270.10; -; 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; 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 PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..1227
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000165798"
SQ SEQUENCE 1227 AA; 137745 MW; A196472460B0B1DF CRC64;
MPPLIESVVL QPLIAPIDPG FDGRRSRRIE RRSFARIKDA IDLPLLIETQ LKSFEWFKRE
GLRELFDEIS PITDFTGKNL ELHFREYTFG EPRYDEFECR DRDLTYAAPL RVKVELRILT
TGEIKESEIF LGDFPMMTDN GTFVYNGAER VVVSQLIRSP GVYFKDEKDP TSGRALHTAK
LIPNRGAWLE FETNKRDVIS VKVDRKRKIP VTILLRAISA WIANEDGSGR WAPDNELDKY
GHNEHLIELF RHVDTVAEHL YIQATIDKDP SHNAKEALLE LYKRLRPGDP PTLENARTLI
ESLLFNPRRY DLAKVGRYKL NKNLWERDAR RDGPKAPDLS VRVLLPRDIF RIVEQMILLN
NGYGRPDDID HLGNRRVRTV GELIQQQFRV GLLRLERVVK ERMSLQDPAS ATPNGLINIR
PVVAAMREFF GGSQLSQFMD QTNPLAELTN KRRLSALGPG GLSRDRAGFE VRDVHHSHYG
RICPVETPEG PNIGLIGTMS TFARVNEMGF LETPYRKVYN SIDNAQVWRE KGILLRDVRD
LRTGDLIAAK GTRVDDQIAR QITIGLLRGQ ILREDVVDPN TGELIAEAGT EINRALAERI
VNLPMKQIKI RPVVSQEVDY LSADEEDRFV IVQANAPLDE HNRFLDTTVS CRFGEDFVTE
RVERVDYMDV SPKQVVSVST SLIPFLEHDD ANRALMGSNM QRQAVPLLRP DAPIVGTGME
YRTARDSGQV VVARRDGVVV SATGNRIIVE EDDGKRTEYR LRKFMRSNQD TCINQRPSVV
RGQQVRAGDV IADSSSTDQG ELALGQNVLV AYMPWEGGNF EDAILVSERL VREDIFTSIH
IEKYEVEARD TKLGPEEITR DIPNVGQDSL RNLDERGIIY IGAEVQPNDI LVGKITPKGE
TDLTAEERLL RAIFGEKARE VKDSSLRVPN GVRGKVIDVK VFSRSEGAEL PVGVNQTVRV
LLCQKRKISA GDKMAGRHGN KGVVSRVLPM EDMPFLPDGR PVDIILNPIG VPSRMNIGQI
LETHLGWAAA RLGFRVATPV FDGAHEDQIK DLLVQAGLPA DGKVTLYDGR TGEKFDHPVT
VGYAYMLKLA HLVEDKIHAR STGPYSLVTQ QPLGGKAQFG GQRFGEMEVW ALEAYGAAYT
LQEMLTVKSD DVVGRVKTYE AIVKGEPIQE AGVPESFKVL IKELQSLGLS VEVLSADEKP
VELSDDLDSD IGALEGINLS GMERGEF
