RPOB_CUTAK
ID RPOB_CUTAK Reviewed; 1159 AA.
AC Q6A6K6;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=PPA1884;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT83607.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6A6K6; -.
DR SMR; Q6A6K6; -.
DR STRING; 267747.PPA1884; -.
DR PRIDE; Q6A6K6; -.
DR EnsemblBacteria; AAT83607; AAT83607; PPA1884.
DR KEGG; pac:PPA1884; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_11; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000000603; 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; Transcription;
KW Transferase.
FT CHAIN 1..1159
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000224092"
FT REGION 1132..1159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 128430 MW; 1A6DE78926EA6C61 CRC64;
MAATRTASKN TSAISPQSGR ISFAKIHEPL EVPNLLDLQV ESFNWLVGNE IWQSRVDAAL
AEGRTDINTK SGLEEIFEEI SPIEDYSQTM SLSFRDHRFE DPKHSVDECK DRDTTYAAPL
FVTAEFMNNE TEEIKSQTVF IGDFPLMTSK GTFIINGTER VVVSQLVRSP GVYFEKTADK
TSDKDIFTCK VIPSRGAWLE FAIDKRDTVG VRLDRKRKQN VTVFLKALGW TADRILEEFG
THESIRQTLE KDHGVETQDQ ALLDIYKKLR PGEPPSRDAA QQLLENYYFN PKRYDLAKVG
RYKINKKLGL SLPFDQQVLT VDDIVAAIHF VCALHEGTAI LPREGQDDIV VEPDDIDHFG
NRRLRTVGEL IQNQLRTGLS RMERVVRDRM TTQDIEAITP QTLINIRPVT AAIKEFFGTS
QLSQFMDQNN PLAEMTHKRR LSALGPGGLS RDRAGMEVRD VHPSHYGRMC PIETPEGPNI
GLIGSLASFA RVNAFGFIET PYRKVVDGHV TDEVVYLTAD EEDRHVIAQA NAKLDDDGHF
ANDRVLVRQR HGEADEVPSS EVDYMDVSPR QMVSVASALI PFLEHDDASR ALMGANMQRQ
AVPLVRTEAP FVGTGMEYRC AVDVGDVTLA EKAGSVLSVS ADLIDIACDD GTYQTYKLEK
FRRSNAGTCI NQRPLVKVGQ RVEVGTPLAD GPSTDNGELA LGRNMLAAFM PWQGLNYEDA
IILSQRIVSD DVLTSIHIEE HEVDARDTKL GAEEITRDIP NVSEDMLANL DENGIVRIGA
EVGTGDILVG KVTPKGETEL TPEERLLRAI FGEKAREVRD TSLKVPHGEE GTVIGVRIFD
TENGDELAPG VNQMVRVYVA QKRKISIGDK LAGRHGNKGV ISKILPVEDM PFLPDGTPVD
IILNPLGVPS RMNVGQVLEM HLGWIAHSGW DITQAEGDWA ERLREVGLID IPEESRLATP
VFDGATEQEI TGLLQYGHPT RDGEMLVDTD GKATLFDGRT GEPFPSKVGV GYMYMLKLHH
LVDDKIHARS TGPYSMITQQ PLGGKAQFGG QRFGEMEVWA MEAYGAAWAL QELLTIKSDD
VPGRVKVYEA IVKGENIPEP GIPESFKVLV KEMKSLCLNV EVLNSEGQEI DLRGSEEDTR
SGLGIDIGRR PGADNAMAD
