ID   RPOB_LISIN              Reviewed;        1184 AA.
AC   Q92F22;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 116.
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=lin0285;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
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; AL596164; CAC95518.1; -; Genomic_DNA.
DR   PIR; AF1468; AF1468.
DR   RefSeq; WP_010990308.1; NC_003212.1.
DR   AlphaFoldDB; Q92F22; -.
DR   SMR; Q92F22; -.
DR   STRING; 272626.lin0285; -.
DR   EnsemblBacteria; CAC95518; CAC95518; CAC95518.
DR   GeneID; 61169287; -.
DR   KEGG; lin:rpoB; -.
DR   eggNOG; COG0085; Bacteria.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000002513; 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   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..1184
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047915"
FT   REGION          1160..1184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1165..1184
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1184 AA;  132606 MW;  A93A171CAB30BBC3 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 KIYAPNDDEK
     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 ARDAKTVLYD
     GRSGEAFDNR ISVGVMYMIK LAHMVDDKLH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME
     VWALEAYGAA YTLQEILTIK SDDVVGRVKT YEAIVKGESV PEPGVPESFK VLIKELQSLG
     MDVKMLSADE EEIEMRDMDD DDFTNQNDAF NIVQPENAAT EKTE