ID   RPOB_AMYMS              Reviewed;        1167 AA.
AC   Q9L637; G0FUS6;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2013, sequence version 2.
DT   03-AUG-2022, entry version 94.
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};
GN   OrderedLocusNames=RAM_03350, AMES_0654;
OS   Amycolatopsis mediterranei (strain S699) (Nocardia mediterranei).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=713604;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=S699;
RA   Pogosova-Agadjanyan E.L., Floss H.G., Yu T.;
RT   "Toward understanding the rifamycin-resistance mechanism: DNA-dependent RNA
RT   polymerase beta-subunit activity in Amycolatopsis mediterranei S699.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S699;
RX   PubMed=21914879; DOI=10.1128/jb.05819-11;
RA   Verma M., Kaur J., Kumar M., Kumari K., Saxena A., Anand S., Nigam A.,
RA   Ravi V., Raghuvanshi S., Khurana P., Tyagi A.K., Khurana J.P., Lal R.;
RT   "Whole genome sequence of the rifamycin B-producing strain Amycolatopsis
RT   mediterranei S699.";
RL   J. Bacteriol. 193:5562-5563(2011).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S699;
RX   PubMed=23012281; DOI=10.1128/jb.01295-12;
RA   Tang B., Zhao W., Zheng H., Zhuo Y., Zhang L., Zhao G.P.;
RT   "Complete genome sequence of Amycolatopsis mediterranei S699 based on de
RT   novo assembly via a combinatorial sequencing strategy.";
RL   J. Bacteriol. 194:5699-5700(2012).
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; AF242549; AAF60349.1; -; Genomic_DNA.
DR   EMBL; CP002896; AEK39162.1; -; Genomic_DNA.
DR   EMBL; CP003729; AFO74190.1; -; Genomic_DNA.
DR   RefSeq; WP_014466582.1; NC_018266.1.
DR   AlphaFoldDB; Q9L637; -.
DR   SMR; Q9L637; -.
DR   STRING; 713604.RAM_03350; -.
DR   PRIDE; Q9L637; -.
DR   EnsemblBacteria; AEK39162; AEK39162; RAM_03350.
DR   KEGG; amm:AMES_0654; -.
DR   KEGG; amn:RAM_03350; -.
DR   PATRIC; fig|713604.12.peg.695; -.
DR   HOGENOM; CLU_000524_4_3_11; -.
DR   OMA; FMTWEGY; -.
DR   OrthoDB; 9601at2; -.
DR   Proteomes; UP000006138; 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; 1.
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; Reference proteome;
KW   Transcription; Transferase.
FT   CHAIN           1..1167
FT                   /note="DNA-directed RNA polymerase subunit beta"
FT                   /id="PRO_0000047851"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        1139
FT                   /note="D -> G (in Ref. 1; AAF60349)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1167 AA;  129354 MW;  FB52392C70A34D2B CRC64;
     MAVSPANQAT AATTSAESRS EATGIPGAPK RVSFAKIREP LNTPNLLDVQ IQSFQWFTGD
     EAWFQRRVEE GEENPVGGLE EVLNEISPIE DFSGSMSLSF SAPRFDEVKA SIEECKDKDM
     TYAAPLFVTA EFVNNNTGEI KSQTVFLGDF PVMTDKGTFV INGTERVVVS QLVRSPGVYY
     SKDIDKTSDK DVFSVRVIPS RGAWLEFDVD KRDTVGVRID RKRRQPVTVL LKALGWTTEA
     IRERFSFSET LLATLEKDHT AGTDEALLDI YRKLRPGEPP TKESAQTLLE NLFFKAKRYD
     LAKVGRYKVN KKLGLSTPIE NGTLTEEDIV TIIEYLVRLH AGEDKMTAAN NTEIPVETDD
     IDHFGNRRIR TVGELIQNQI RVGLSRTERV VRERMTTQDV EAITPQTLIN IRPIGAAIKE
     FFGTSQLSQF MQQTNPIDGL THKRRLNALG PGGLSRERAG MEVRDVHPSH YGRMCPIETP
     EGPNIGLIGS LCSYARVNPF GFIETPYRKV VEGRVTDQID YLTADEEDRF VKAQANAPIS
     DDGTFIEDRV MARRKGGEVE LIDPLDIDYM DVSPRQMVSI ATAMIPFLEH DDANRALMGA
     NMQRQAVPLL RSQAPYVGTG VELRAAIDSG DMLVAEQSGV VEELSADLIT VMHDDGTRKS
     YSLYKFRRSN HGTCFNHRPI VNEGDRIEAG QVIADGPSTE NGEVALGKNL LVAVMPWEGH
     NYEDAIILSE RLVQDDVLTS IHIEEHEIDA RDTKLGAEEI TRDIPNVSEE VLADLDERGI
     IRIGAEVRDG DILVGKVTPK GETELTPEER LLRAIFGEKA REVRDTSLKV PHGETGKVIG
     IRVFSREDDD ELPPGVNELV RVYVAQKRKI QPGDKLAGRH GNKGVIGKIL PVEDMPFMED
     GTPVDIILNT HGVPRRMNIG QILELHLGWL ASQGWTIEGD PDWAKNLSAE LRDVAPGTNT
     ATPVFDGAKE EELTGLLSAT KPNRDGERMV KENGKANLFD GRSGEPYPYP VAVGYMYILK
     LHHLVDDKIH ARSTGPYSMI TQQPLGGKAQ FGGQRFGEME CWAMQAYGAA YTLQELLTIK
     SDDVVGRVKV YEAIVKGENI PEPGIPESFK VLLKELQSLC LNVEVLSSDG SSIEMRDSDD
     EDLERAAANL GINLSRNESP SVDDVVH