RPOB_LAWIP
ID RPOB_LAWIP Reviewed; 1373 AA.
AC Q1MPW8;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=LI0905;
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00;
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM180252; CAJ54959.1; -; Genomic_DNA.
DR RefSeq; WP_011526988.1; NC_008011.1.
DR AlphaFoldDB; Q1MPW8; -.
DR SMR; Q1MPW8; -.
DR STRING; 363253.LI0905; -.
DR KEGG; lip:LI0905; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR Proteomes; UP000002430; 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; -; 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 DNA-directed RNA polymerase; Nucleotidyltransferase; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1373
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000300337"
SQ SEQUENCE 1373 AA; 153863 MW; 40B6669F4919E8D6 CRC64;
MVQLTKQFGK IKVEVPIPHL LNLQVDSYKK FLQEGLLEPL PEEGLESVFR SVFPIEDFNR
TSSLEFVNYK IGEPKYDQAE CIAKGLTYEA PIRIKVRLII YDVDSDTESR TVHDIKEQDI
YFGTLPLMTE KGTFIINGTE RVIVNQLQRS PGIIFEHDSG KTHASRKVLY SCRIIPMRGS
WLDFDFDHKD ILYVRIDRRR KMPATILLKA MGMGKQDILN FFYKKETYIL DNDGRIKWKF
DPSLFRKDIA YTDILDNDNN LLVAAGKTIT KRVWRQMEAS GLEAFEVDPS TVIGQFLAED
IIDTSTGEIL AESAEEITEG LIQTFRDAGI TTFTVLHTRG NDTSSSIRDT LVQDKIPTTE
KAQEEIYRRL RPSSPPTPEI AASFFDNLFR NNSYYDLSPV GRYKLNQRLD NYENATLRTL
SDNDILEAIK LLTHLKDSHG PADDIDHLGN RRVRLVGELV ENQYRIGLVR MERAIKERMS
IQEVATLMPH DLINPKPVAA LLKEFFGTSQ LSQFMDQTNS LSEVTHKRRL SALGPGGLTR
ERAGFEVRDV HVSHYGRICP IETPEGPNIG LIVSLTTYAK VNDYGFIETP YRVVRNGYVT
DEIIHLDASC EFSEVIAQAN ASIDSEGRLI DDYVTTRARG DVLMSAREEV TLMDISPSQM
VSISAALIPF LEHDDANRAL MGSNMQRQAV PLLRSERPLV GTGMEVDVAH DSGSCILAEG
DGIIRYADAN RIIVSYDDPN LYPEFGGVRA YDLLKYHKSN QNFCFGQRPS CIPGQIVKKG
EVLADGPAIR DGGLALGKNL VVAFMPWCGY NFEDSILISE RVVKEDTYTS VHIEEFEIVA
RDTKLGPEEI TRDIPNVGEE MLSNLDENGI IRIGAAVKPE DILVGKITPK GETQLTPEEK
LLRAIFGDKA RDVKNTSLKV PPGIEGTVID VKVFNRRSGE KDDRTRLIED YEISLMDSKE
QNYIKSITQR MKEKILPLIN GKQLGTTILG KGKGEVLAEE NSAITPELLD SLPLKKLEGA
FKSKELNETI TEMLSQYEKQ INYIKTIYDS KRGKVTEGDD LPPGVIRMVK VHIAVKRKLA
VGDKMAGRHG NKGVVSCILP EEDMPFFADG SPVDIVLNPL GVPSRMNIGQ IMETHLGWAA
KELGQQLNNM VEQGVAIQSL REQVKSVFES PEISAEIDAM DDDTFRTSVQ KLKKGIITMT
PVFDGAGESE VWDWLAKAGL PSDGKAILYD GRTGEAFKNR VTTGVMYILK LHHLVDEKIH
ARSTGPYSLV TQQPLGGKAQ FGGQRLGEME VWALEAYGAS YLLQEFLTVK SDDVSGRVKM
YEKIVKGDNF LEAGLPESFN VLVKELMSLG LNVTLHQEEG KKKPKRTGLI DKE
