RPOB_LEUCK
ID RPOB_LEUCK Reviewed; 1204 AA.
AC B1MVW8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=LCK_01548;
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20;
RX PubMed=18281406; DOI=10.1128/jb.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA83372.1; -; Genomic_DNA.
DR RefSeq; WP_004904425.1; NC_010471.1.
DR AlphaFoldDB; B1MVW8; -.
DR SMR; B1MVW8; -.
DR STRING; 349519.LCK_01548; -.
DR EnsemblBacteria; ACA83372; ACA83372; LCK_01548.
DR GeneID; 61101420; -.
DR KEGG; lci:LCK_01548; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002166; 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; Transcription;
KW Transferase.
FT CHAIN 1..1204
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141707"
SQ SEQUENCE 1204 AA; 134455 MW; E8B957F2C9DE9DD8 CRC64;
MAGHLVKYGK HRTRRSYASI KEVLDVPNLI EIQTASYQWF LDEGIKEMFG DIMPIDDFQG
TLSLEYVDYQ LMEPKYNIDE AREHDANYSA PLHVTLRLTN HETGEIKSQD VFFGEFPLMT
EQGTFIINGA ERVIVSQLVR SPGIYYNQEN DKNGRPRYGT TVIPNRGAWL EYETDAKGIA
NVRIDRTRKL LMTELVRALG FGSDSDIIDI FSDQYDALNM TLEKDVHKDM SDSRVEEALK
DVYERLRPGE PKTADSSRAL LVARFFDPKR YDLASVGRYK INKKLSLKTR LLNQTLAETL
ADPDSGEVIA EKGTLVDKTV MSKLSPFLDR EDFKTTTYTP SGDAVLEEPV TLQKIKIESP
ENPEKTLLLI GNGHIDENDR TVRPADILAG MNYFLNLQEG IGNVDDIDHL GNRRIRSVGE
LLQNQFRIGL TRMERVVRER MSIQDANTVT PQQLINIRPV VAAVKEFFGS SQLSQFMDQT
NPLGEMNHKR RLSALGPGGL TRDRAGVEVR DVHYTHYGRI DPIETPEGPN IGLINSLATY
GRINKYGFIE TPYRRVDWTT HMVTDKIDYL TADEEDNYIV AQANSPLNDD GSFVHDTVMA
RFGEENIETP IDRIDYMDVS PKQVVSVGTA AIPFLENDDS NRALMGANMQ RQAVPLLDPH
APLVGTGIEY KAAHDSGVAM ISRAAGVVEY VDGRQIRVRR EDGQLDTYEL MKFRRSNGGK
NYNQKPIVHE GEHVEADEVL ADGPSMEKGE LALGQNPLIA FMTWQGYNFE DAIVLNERLV
REDVYTSIHI EEYDSEARDT KLGPEEMTRE IPNTGEDQLK DLDADGIIRV GAEVHDGDIL
VGKVTPKGVT ELSAEERLLH AIFGEKAREV RDTSLRVPHG GGGVVQNVRI YTPENGDELA
PGVNMMVRVY IAQKRKIQVG DKMAGRHGNK GTVSVVVPEE DMPYMPDGTP IDILLSPMGV
PSRMNIGQVL ELHLGFAAKK LGIHVASPVF DGASDDEIEA ALREAGLPQD GKSVVYDGRT
GEAFDKRVGV GVMHYMKLAH MVDDKIHARS IGPYSLVTQQ PLGGKAQFGG QRFGEMEVWA
LEAYGAAYTL QEILTYKSDD VAGRVKVYES IIKGEPIPRP GVPESFRVLV KELQALGLDM
QVLDNAGDEV ELRQMDEDDS ILPVDALEKL VRSNPDLLNK EDEEVAAAFS KVESRDNTEV
TDEN