ID D7GJ17_PROFC Unreviewed; 1158 AA.
AC D7GJ17;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000256|ARBA:ARBA00021955, ECO:0000256|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000256|ARBA:ARBA00012418, ECO:0000256|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000256|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000256|HAMAP-Rule:MF_01321,
GN ECO:0000313|EMBL:CBL56089.1};
GN OrderedLocusNames=PFREUD_05600 {ECO:0000313|EMBL:CBL56089.1};
OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM
OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Propionibacterium.
OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL56089.1, ECO:0000313|Proteomes:UP000000936};
RN [1] {ECO:0000313|EMBL:CBL56089.1, ECO:0000313|Proteomes:UP000000936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1
RC {ECO:0000313|Proteomes:UP000000936};
RX PubMed=20668525; DOI=10.1371/journal.pone.0011748;
RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S.,
RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P.,
RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C.,
RA Lortal S.;
RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy
RT actinobacterium with food and probiotic applications.";
RL PLoS ONE 5:E11748-E11748(2010).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031}.
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:0000256|ARBA:ARBA00024550,
CC ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031};
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:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU363031}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000256|HAMAP-Rule:MF_01321, ECO:0000256|RuleBase:RU000434}.
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; FN806773; CBL56089.1; -; Genomic_DNA.
DR AlphaFoldDB; D7GJ17; -.
DR STRING; 754252.PFREUD_05600; -.
DR KEGG; pfr:PFREUD_05600; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_11; -.
DR Proteomes; UP000000936; 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:DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1100.10; -; 1.
DR Gene3D; 2.30.150.10; DNA-directed RNA polymerase, beta subunit, external 1 domain; 1.
DR Gene3D; 2.40.270.10; DNA-directed RNA polymerase, subunit 2, domain 6; 1.
DR Gene3D; 3.90.1800.10; RNA polymerase alpha subunit dimerisation domain; 1.
DR Gene3D; 3.90.1110.10; RNA polymerase Rpb2, domain 2; 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 NCBIfam; TIGR02013; rpoB; 1.
DR PANTHER; PTHR20856; DNA-DIRECTED RNA POLYMERASE I SUBUNIT 2; 1.
DR PANTHER; PTHR20856:SF20; DNA-DIRECTED RNA POLYMERASE SUBUNIT BETA; 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 SUPFAM; SSF64484; beta and beta-prime subunits of DNA dependent RNA-polymerase; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase {ECO:0000256|ARBA:ARBA00022478,
KW ECO:0000256|HAMAP-Rule:MF_01321};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_01321}; Reference proteome {ECO:0000313|Proteomes:UP000000936};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01321};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01321}.
FT DOMAIN 34..404
FT /note="RNA polymerase beta subunit protrusion"
FT /evidence="ECO:0000259|Pfam:PF04563"
FT DOMAIN 167..359
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04561"
FT DOMAIN 418..486
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04565"
FT DOMAIN 496..562
FT /note="DNA-directed RNA polymerase beta subunit external 1"
FT /evidence="ECO:0000259|Pfam:PF10385"
FT DOMAIN 627..1041
FT /note="DNA-directed RNA polymerase subunit 2 hybrid-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00562"
FT DOMAIN 1043..1117
FT /note="RNA polymerase Rpb2"
FT /evidence="ECO:0000259|Pfam:PF04560"
SQ SEQUENCE 1158 AA; 128722 MW; 2B570BD0109CB0A7 CRC64;
MAASRTALNN SDVVSTTGRI SFAKIREPLG IPNLLDLQVK SFNWLVGNEN WQNEVDQALS
EGRTDVNTKS GLEEIFEEIS PIEDFSQTMS LSFRDHRFEE PKYTIEECKD RDATYAAPLF
VTAEFMNNDT GEIKSQTVFI GDFPLMTDKG TFIITGTERV VVSQLVRSPG VYFEQTPDKT
SDKDIFTCKV IPSRGAWLEF EIDKRDTVGV RLDRKRKQNV TVLLKALGWT EERILEEFGE
YESIRMTMEK DHVTTQDEAL LDIYRKLRPG EPPARDAAQT LLDNFYFNPK RYDTAKVGRY
KINKKLGLSL PYDQQVLTMD DIVAAIHYIC ALHEGKTELA DGLPVEPDDI DHFGNRRVRT
VGELIQNQLR TGLGRMERVV RDRMTTQDIE AITPQTLINV RPVTAALKEF FGTSQLSQFM
DQNNPLAELT HKRRLSAVGP GGLSRDRAGM EVRDVHPSHY GRMCPIETPE GPNIGLIGSL
ASFARVNAFG FIETPYRKVD KGLVTDHIDY LTADEEDRFV IAQANATMND KGELTEDRVL
VRVSHGDVDL VPADEVDYID VSARQMVSVG SALIPFLEHD DSSRALMGAN MQRQAVPLVR
NESPYVGTGM EYRAAVDVGE VTLASKPGTV TGVTGDLIDI ACDDGTYQTF KLEKFQRSNA
GTCVNQRPIV TPGQHVEAGT PLADGPCTDQ GELALGRNLL CAFMPWRGLN YEDAIIISQR
VVSEDILTSI HIEEYEVDAR DTKLGPEEIT HDIPNVSDDM IASLDDRGIV RIGAEVRPGD
ILVGKVTPKG ETELTPEERL LRAIFGEKAR EVRDTSMKVP HGEEGTVIGV RIFDREENDE
LPPGVNQMVR VYVAQKRKVQ VGDKLAGRHG NKGVISRILP IEDMPFMADG TPVDIMLNPL
GVPSRMNLGQ VLEMHLGWIA HSGWDLGDAT DPWAEHLREV GLEHVDGDVR LATPVFDGAE
EHEITGLLAH GLPNRDGDHI VDSDGKTTLF DGRTGEEFPE EVGVGYMYML KLHHLVDDKI
HARSTGPYSM ITQQPLGGKA QFGGQRFGEM EVWALEAYGA AWALQEMLTI KSDDVAGRVK
VYEAIVKGEN IPEPGIPEGF KVLVQEMKSL CLNVEVLGSD GAVIDLRETE DDYRTVDELG
IDLSRRPGTD SYKLESEG
//
