RPOB_LISMO
ID RPOB_LISMO Reviewed; 1184 AA.
AC Q9RLT9;
DT 21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=lmo0258;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS RIFAMPICIN RESISTANT.
RC STRAIN=ATCC 35152 / LMG 10470 / NCTC 7973;
RX PubMed=10449475; DOI=10.1128/jcm.37.9.2913-2919.1999;
RA Morse R., O'Hanlon K., Virji M., Collins M.D.;
RT "Isolation of rifampin-resistant mutants of Listeria monocytogenes and
RT their characterization by rpoB gene sequencing, temperature sensitivity for
RT growth, and interaction with an epithelial cell line.";
RL J. Clin. Microbiol. 37:2913-2919(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35152 / LMG 10470 / NCTC 7973;
RX PubMed=12361249; DOI=10.1099/00207713-52-5-1477;
RA Morse R., O'Hanlon K., Collins M.D.;
RT "Phylogenetic, amino acid content and indel analyses of the beta subunit of
RT DNA-dependent RNA polymerase of Gram-positive and Gram-negative bacteria.";
RL Int. J. Syst. Evol. Microbiol. 52:1477-1484(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
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; Y16468; CAB56706.1; -; Genomic_DNA.
DR EMBL; AL591974; CAD00785.1; -; Genomic_DNA.
DR PIR; AC1107; AC1107.
DR RefSeq; NP_463789.1; NC_003210.1.
DR RefSeq; WP_003723045.1; NZ_CP023861.1.
DR AlphaFoldDB; Q9RLT9; -.
DR SMR; Q9RLT9; -.
DR STRING; 169963.lmo0258; -.
DR PaxDb; Q9RLT9; -.
DR EnsemblBacteria; CAD00785; CAD00785; CAD00785.
DR GeneID; 987342; -.
DR KEGG; lmo:lmo0258; -.
DR PATRIC; fig|169963.11.peg.266; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_1_9; -.
DR OMA; FMTWEGY; -.
DR PhylomeDB; Q9RLT9; -.
DR BioCyc; LMON169963:LMO0258-MON; -.
DR BRENDA; 2.7.9.6; 3045.
DR Proteomes; UP000000817; 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:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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 Antibiotic resistance; DNA-directed RNA polymerase; Nucleotidyltransferase;
KW Reference proteome; Transcription; Transferase.
FT CHAIN 1..1184
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047917"
FT REGION 1160..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 473
FT /note="D -> N (rifampicin resistant)"
FT VARIANT 479
FT /note="G -> D (rifampicin resistant)"
FT VARIANT 483
FT /note="H -> L (rifampicin resistant)"
FT VARIANT 483
FT /note="H -> Y (rifampicin resistant)"
FT VARIANT 528
FT /note="L -> F (rifampicin resistant)"
FT VARIANT 530
FT /note="N -> Y (rifampicin resistant)"
SQ SEQUENCE 1184 AA; 132604 MW; 58B4427F44A7290F CRC64;
MSGHSGHDVK YGRHRTRRSF ARISEVLELP NLIEIQTASY QWFLDEGLRE MFRDISPIED
FAGNLSLEFI DYDLGEPKYS VEESKNRDAN YAAPLRVKLR LINKETGEVK DQEVFMGDFP
LMTEMGTFII NGAERVIVSQ LVRSPGVYFN GKLDKNGKKG FGSTVIPNRG AWLEYETDAK
DVVHVRIDRT RKLPVTVLLR ALGFGSDQEI IDLIGDNDYL RNTLEKDNTD NAEKALLEIY
ERLRPGEPPT VDNARSLLVS RFFDPKRYDL ASVGRYKINK KLHLKNRLFN QTLAETLVDP
ETGEIIASKG DILDRRNLDQ IIPNLENGVG FRTLRPTDGV MEDSVLVQSI KIYAPNDEEK
EINIIGNAYI EENVKHITPS DIISSISYFF NLLHGVGDTD DIDHLGNRRL RSVGELLQNQ
FRIGLSRMER VVRERMSIQD MTTITPQQLI NIRPVVASIK EFFGSSQLSQ FMDQTNPLGE
LTHKRRLSAL GPGGLTRERA GYEVRDVHYS HYGRMCPIET PEGPNIGLIN SLSSFAKVNK
FGFIETPYRR VDPETNRVTD KIDYLTADEE DNYVVAQANS KLDEQGTFTE EEVMARFRSE
NLAVEKERID YMDVSPKQVV SVATACIPFL ENDDSNRALM GANMQRQAVP LMHPEAPFVG
TGMEHVSAKD SGAAVTAKHD GIVEHVEARE IWVRRVSLVD GKEVTGGIDK YTLRKFVRSN
QGTCYNQRPN VAEGDRVVKG EILGNGPSMD SGELALGRNV LVAFMTWDGY NYEDAIIMSE
RLVKDDVYTS IHIEEFESEA RDTKLGPEEM TRDIPNVGED ALRDLDERGI IRVGAEVKDN
DLLVGKVTPK GVTELTAEER LLHAIFGEKA REVRDTSLRV PHGGGGIVLD VKIFTREAGD
ELPPGVNQLV RVYIVQKRKI HEGDKMAGRH GNKGVISRIL PEEDMPFMPD GTPVDIMLNP
LGVPSRMNIG QVLELHLGMA ARALGIHVAT PVFDGANEED VWSTVEEAGM ARDAKTILYD
GRSGEAFDNR ISVGVMYMIK LAHMVDDKLH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME
VWALEAYGAA YTLQEILTIK SDDVVGRVKT YEAIVKGESV PEPGVPESFK VLIKELQSLG
MDVKMLSADE EEIEMRDMDD DDFTNQNDAF NIVQPENAAA EKTE