RPOB_STRMK
ID RPOB_STRMK Reviewed; 1388 AA.
AC B2FQ38;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Smlt0898;
OS Stenotrophomonas maltophilia (strain K279a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=522373;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K279a;
RX PubMed=18419807; DOI=10.1186/gb-2008-9-4-r74;
RA Crossman L.C., Gould V.C., Dow J.M., Vernikos G.S., Okazaki A.,
RA Sebaihia M., Saunders D., Arrowsmith C., Carver T., Peters N., Adlem E.,
RA Kerhornou A., Lord A., Murphy L., Seeger K., Squares R., Rutter S.,
RA Quail M.A., Rajandream M.A., Harris D., Churcher C., Bentley S.D.,
RA Parkhill J., Thomson N.R., Avison M.B.;
RT "The complete genome, comparative and functional analysis of
RT Stenotrophomonas maltophilia reveals an organism heavily shielded by drug
RT resistance determinants.";
RL Genome Biol. 9:R74.1-R74.13(2008).
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; AM743169; CAQ44468.1; -; Genomic_DNA.
DR AlphaFoldDB; B2FQ38; -.
DR SMR; B2FQ38; -.
DR STRING; 522373.Smlt0898; -.
DR PRIDE; B2FQ38; -.
DR EnsemblBacteria; CAQ44468; CAQ44468; Smlt0898.
DR KEGG; sml:Smlt0898; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_3_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000008840; 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; 2.40.270.10; -; 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; 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; 3.
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..1388
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141741"
SQ SEQUENCE 1388 AA; 154732 MW; BBD134F661D0F1F6 CRC64;
MEDLMTSYSF TEKKRIRKDF GKQRSILEVP FLLAIQVDSY REFLQENVDP AKRTDHGLHA
ALKSVFPIAS YSGNAALEYV GYKLGEPVFD ERECRQRGMS YGAPLRVTVR LVIYDRESST
KAIKYVKEQE VYLGEIPLMT ENGTFIVNGT ERVIVSQLHR SPGVFFDHDR GKTHSSGKLL
YSARIIPYRG SWLDFEFDPK DALFTRIDRR RKLPVSILLR ALGYSNEEML AEFFEINTFH
INPDEGVQLE LVPERLRGET LGFDLADGDK VIVEAGKRIT ARHIKQLEAS GIAALAVPDD
YIVGRILSHD VVDASTGELL AQANDEITDE QLQAFRKAGV DAVGTLWVND LDRGPYLSNT
LRIDPTKTQL EALVEIYRMM RPGEPPTKDA AQNLFHNLFF TFERYDLSAV GRMKFNRRVG
RKETTGEAVL YDSKYFGERN DEESKRLVAA HGDSSDILDV IKVLTEIRNG RGVVDDIDHL
GNRRVRSVGE MAENVFRVGL VRVERAVKER LSMAESEGLT PQELINAKPV AAAIKEFFGS
SQLSQFMDQN NPLSEVTHKR RVSALGPGGL TRERAGFEVR DVHPTHYGRV CTIETPEGPN
IGLINSLAVY ARTNQYGFLE TPYRKVVDGK VYDEVEFLSA IEENEYVIAQ ANALTDAKGT
LTEQFVPCRF QGESLLKPPA EVHFMDVSPM QTVSIAAALV PFLEHDDANR ALMGANMQRQ
AVPTLRAQKP LVGTGIERAV ARDSGVTVNA RRGGEIVQID AARIVVKVNE EEIVGATDAG
VDIYNLVKYT RSNQNTCINQ RPLVQVGDVI ARGDVLADGP STDIGELALG QNMLIAFMPW
NGYNFEDSIL LSERVVEEDR YTTIHIEELT CVARDTKLGP EEISADIPNV SEQALNRLDE
SGVVYIGAEV RAGDIMVGKV TPKGESQLTP EEKLLRAIFG EKASDVKDSS LRVPPGMDGT
VIDVQVFTRD GIEKDKRARQ IEESEIKRVK KDFDDQFRIL EAAIYMRLRS QIVGKVVNGG
AGLKKGDVIT DAFLDGLKKA DWFALRMKDE DASEAIERAQ KQIQAHEKEF ERRFADKRGK
ITAGDDLAPG VLKMVKVFLA VKRRIQPGDK MAGRHGNKGV VSNVVPVEDM PYMASGETVD
IVLNPLGVPS RMNIGQILEV HLGWAAKGLG RKIQAMMEAQ AAVADLRKFL DDIYNHDDTN
VANRVDLSQF SDEELLRLAR NLTDGVPMAT PVFDGATEAE IKRMLELADL PSSGQTQLYD
GRTGEAFDRH TTVGYMHYLK LNHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME
VWALEAYGAA YTLQEMLTVK SDDVQGRNQM YKNIVDGEHE MVAGMPESFN VLVKEIRSLA
INMELEDN
