ID   RPOB_LISMH              Reviewed;        1184 AA.
AC   B8DEY8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=LMHCC_2373;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK40710.1; -; Genomic_DNA.
DR   RefSeq; WP_003729181.1; NC_011660.1.
DR   AlphaFoldDB; B8DEY8; -.
DR   SMR; B8DEY8; -.
DR   PRIDE; B8DEY8; -.
DR   GeneID; 67409997; -.
DR   KEGG; lmh:LMHCC_2373; -.
DR   HOGENOM; CLU_000524_4_1_9; -.
DR   OMA; FMTWEGY; -.
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_1000165810"
FT   REGION          1160..1184
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1184 AA;  132590 MW;  AB3C0D6E2459936B 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 ARDAKTILYD
     GRSGEAFDNR ISVGVMYMIK LAHMVDDKLH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME
     VWALEAYGAA YTLQEILTIK SDDVVGRVKT YEAIVKGESV PEPGVPESFK VLIKELQSLG
     MDVKMLSADE EEIEMRDMDD DDFTNQNDAF NIVQPENAAA EKTE