RPOB_PORGI
ID RPOB_PORGI Reviewed; 1269 AA.
AC Q7MX27;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=PG_0394;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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; AE015924; AAQ65599.1; -; Genomic_DNA.
DR RefSeq; WP_005873809.1; NC_002950.2.
DR AlphaFoldDB; Q7MX27; -.
DR SMR; Q7MX27; -.
DR STRING; 242619.PG_0394; -.
DR PRIDE; Q7MX27; -.
DR EnsemblBacteria; AAQ65599; AAQ65599; PG_0394.
DR KEGG; pgi:PG_0394; -.
DR PATRIC; fig|242619.8.peg.361; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_10; -.
DR OMA; FMTWEGY; -.
DR OrthoDB; 9601at2; -.
DR BioCyc; PGIN242619:G1G02-369-MON; -.
DR Proteomes; UP000000588; 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; -; 2.
DR Gene3D; 2.40.50.150; -; 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; 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..1269
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047936"
SQ SEQUENCE 1269 AA; 142341 MW; 428D2AB0365AB406 CRC64;
MTPTTNNKRI NFASIKNPLF YPDFLEVQLK SFHDFLQLDT PPERRKKEGL YKVFAENFPI
TDTRNNFVLE FLDYYIDPPK YSIEECLSRG LTYSVPLKAK LKLYCTDPDH EDFATVIQDV
FLGPIPYMTS SGTFVINGAE RVIVSQLHRS PGVFFGQSLH TNGTKLYSAR IIPFKGSWIE
FATDINNVMY AYIDRKKKLP VTTLLRAIGF EADKDILDIF NLAEEVKVTK ANLKKCIGRK
LAARVINTYI DDLSDEDTGE VVSMERITVV VDREVELTED NIEAILNSNT QTILLHRNDS
NTSDYSIIFN TLQKDPCNSE KEALYYVYRQ LRNAEPADDA SAREVITNLF FSDKRYDLGD
VGRYRINKKL NLNIDPDIKV LTNEDIIEII KYLIELVNSK ASVDDIDHLS NRRVRTVGEQ
LYNQFGIGLA RMARTVRDRM NVRDNEVFTP IDLVNAKTIS SVVNSFFGTN ALSQFMDQTN
PLAEITHKRR LSALGPGGLS RERAGFEVRD VHYTHYGRLC PIETPEGPNI GLISSLCVYA
KISDLGFITT PYREVKNGKV DFSDNGLKYY TAEEEEEKTV AQGNAPLDEN GRFVRERVKA
RYESDFPLVT PDEVDLMDVS PTQIASIAAA LIPFLEHDDA NRALMGSNMM RQAVPLLRPE
SPIVGTGIEG KLVKDSRTQI VAERGGEVVF VDASCIKIRY DRTADEEFVS FDDAIVTYYL
PKYRKTNQST TIDLHPICSK GDRVEAGQIL TEGYSTQGGE LALGRNVQVA YMPWKGYNYE
DAIVLNERMV REDFFTSVHV DEYILEVRET KRGLEELTSD IPNVSEDATR DLDENGIVRI
GAHIEPGDIL IGKITPKGES DPTPEEKLLR AIFGDKAGDV KDASLKATPS LRGVVIDTKL
FSKAAKKKSR TSTKEAVSKL DETYAKRQQQ LHERLIDKLT ELTKGKTCCG VKDYLNVELI
KAGSKFAKKD LEALDFNVIQ LSDWTNDAHT NELIKAVAVN YLKHSKEIEA ELRRRKLDET
IGDELPAGIV QMAKVYIAKK RKIQVGDKMA GRHGNKGIVS KIVRQEDMPF LADGTPVDIC
LNPLGVPSRM NLGQIFEAVL AWAGRKMNVK FATPIFDGAS LNDMNEWTDK AGLPRDGKTY
LYDGGTGERF DQPATVGVTY FLKLGHMVDD KMHARSIGPY SLITQQPLGG KAQFGGQRFG
EMEVWALEAF GASHILQEIL TVKSDDVVGR SKAYEAIVKG DPMPTPGIPE SLNVLLHELK
GLGLSFSLD
