RPOB_BIFLO
ID RPOB_BIFLO Reviewed; 1187 AA.
AC Q8G514;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=BL1205;
OS Bifidobacterium longum (strain NCC 2705).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=206672;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCC 2705;
RX PubMed=12381787; DOI=10.1073/pnas.212527599;
RA Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA Zwahlen M.-C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT the human gastrointestinal tract.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
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; AE014295; AAN25011.1; -; Genomic_DNA.
DR RefSeq; NP_696375.1; NC_004307.2.
DR RefSeq; WP_007053735.1; NC_004307.2.
DR AlphaFoldDB; Q8G514; -.
DR SMR; Q8G514; -.
DR STRING; 206672.BL1205; -.
DR EnsemblBacteria; AAN25011; AAN25011; BL1205.
DR KEGG; blo:BL1205; -.
DR PATRIC; fig|206672.9.peg.920; -.
DR HOGENOM; CLU_000524_4_1_11; -.
DR OMA; FMTWEGY; -.
DR PhylomeDB; Q8G514; -.
DR Proteomes; UP000000439; 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..1187
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047864"
FT REGION 1150..1187
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 131716 MW; 8F213D2E73895201 CRC64;
MATESTTNTT TIIARADQHD IDLHKASDRV NFGSIKEPID VPYLLGVQTD SFDWLIGNER
WKARVEEDEK NGTNTVAHTS GLDEVFNEIS PIENFAQTMS LTFSDPYFEE PRHTVQECKE
KDYTYSAPLY VNAEFENGDT GEIKSQTVFM GDFPLQTPHG TFIIGGTERV IVSQLVRSPG
VYFDRQQDRT SDKEVFGAKI IPSRGAWLEF EIDKKDQPQV RVDRKRKQSA IVFLMAIGMT
KSEIAQAFKD YPLVLDALEK ETLETQDEAL VDLYRKIRPA DTPTPEAGKN LLDSFYFNTK
RYDLARVGRY KINRKLGVEA DFNDRSLHQE DIIATIKYLV ALHDGAATFP GKRNGEDVDL
RVDVDDIDHF GNRRIRQVGE LIQNQLRTGL SRMERVVRER MTTQDAEAIT PQSLINIRPV
NATIKEFFGT SQLSQFMDQN NPLSGVTNKR RLSALGPGGL SRDRASMEVR DVHPSHFGRM
CPIESPEGPN IGLIGSLATF GRVNPFGFIE TPYRKVVNGH VTDEVEYMTA DRDLDHVIAQ
ANQELDENGN FVQKSALARV GEEEAVDVPV SSVDYMDVSP RQMVSLGASL IPFLEHDEGH
RALMGTNMQR QAVPLIESER PLVGTGSEWR AANDSGDVIK SEKDGVVTYV SADLIRVMND
DGTTSSYKLA KFQRSNQTTC YNQRPIVHDG ERVEAGSVMA DGPAIQNGDL ALGKNLLIAF
MPWNGYNYED AVIISQRLVQ DDTLSSIHIE EYEIDARETK LGAEEITRDL PNVGEDAVAN
LDERGIIRIG AEVEAGDILV GKVTPKGETE LTPEERLLRA IFGEKSREVR DTSLRVPHGE
TGTVIGVKEI TREDAEEDGD ELPNGVNQMI RVYIAQHRKI TVGDKLSGRH GNKGCISRIL
PEEDMPFLAD GTPVDIMLNP LGVPSRMNLG QVLELHLGWI AHSGWDISLD PNLEAEWKKL
IPSGAEKAEP NTPVATPVFD GVKPEVLKGL LSTTLPNRDG DRLVGPDGKA TLFDGRTGEP
YTKPISVGYM YMLKLHHLVD DKIHARSTGP YSMITQQPLG GKAQFGGQRF GEMEVWALEA
YGAAYTLHEM MTTKSDDVDG RVRVYGAIVK GDNLPPAGIP ESFKVLLKEM QSLSLNVEVL
NAEGVAIDMK DEDDDPASSA DDLGFNIGAR PDAAAKEDQK AEEPEYQ
