RPOB_XANCB
ID RPOB_XANCB Reviewed; 1387 AA.
AC B0RU89;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
GN OrderedLocusNames=xcc-b100_3466;
OS Xanthomonas campestris pv. campestris (strain B100).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=509169;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B100;
RX PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA Puehler A.;
RT "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT the reconstruction of metabolic pathways involved in xanthan
RT biosynthesis.";
RL J. Biotechnol. 134:33-45(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; AM920689; CAP52831.1; -; Genomic_DNA.
DR AlphaFoldDB; B0RU89; -.
DR SMR; B0RU89; -.
DR KEGG; xca:xcc-b100_3466; -.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000001188; 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; 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; Transcription;
KW Transferase.
FT CHAIN 1..1387
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000141749"
SQ SEQUENCE 1387 AA; 154855 MW; E1B4866242D89F89 CRC64;
MEDLMTSYSF TEKKRIRKDF GKQRSILEVP FLLAIQVDSY REFLQEDVEP NKRKDLGLHA
ALKSVFPISS YSGNAALEYV GYKLGEPVFD ERECRQRGMS YGAPLRVTVR LVIYDRESST
KAIKYVKEQE VYLGEIPLMT ENGTFIVNGT ERVIVSQLHR SPGVFFDHDR GKTHSSGKLL
YSARIIPYRG SWLDFEFDPK DALFTRIDRR RKLPVSILLR ALGYNNEEML AEFFEINTFH
INPDEGVQLE LVPERLRGET LNFDLADGDK VIVEAGKRIT ARHVKQLEAA GVAALAVPDD
YLVGRILSHD VVDGSTGELL ANANDEISED QLAAFRKAGV DAVGTLWVND LDRGPYLSNT
LRIDPTKTQL EALVEIYRMM RPGEPPTKEA AQNLFHNLFF TFERYDLSTV GRMKFNRRVG
RKEVLGESVL YDKKYFAERN DEESKRLVAE HADTSDILEV IKVLTEIRNG RGVVDDIDHL
GNRRVRSVGE MAENVFRVGL VRVERAVKER LSMAESEGLT PQELINAKPV AAAIKEFFGS
SQLSQFMDQN NPLSEVTHKR RVSALGPGGL TRERAGFEVR DVHPTHYGRV CTIETPEGPN
IGLINSLAVF ARTNQYGFLE TPYRKVLDGK VSDDVEYLSA IEENEYVIAQ ANALTDAKNM
LTEQFVPCRF QGESLLKPPA EVHFMDVSPM QTVSVAAALV PFLEHDDANR ALMGANMQRQ
AVPTLRSQKP LVGTGIERAV ARDSGVTVNA RRGGVIEQID AARIVVKVNE AEIGGGTDAG
VDIYNLIKYT RSNQNTCINQ RPLVNVGDVI ARGDVLADGP STDIGELALG QNMLIAFMPW
NGYNFEDSIL LSERVVEEDR YTTIHIEELT CVARDTKLGP EEISADIPNV SEQALNRLDE
SGVVYIGAEV RAGDIMVGKV TPKGESQLTP EEKLLRAIFG EKASDVKDSS LRVPPGMDGT
VIDVQVFTRD GIEKDKRARQ IEESEIKRVK KDFDDQFRIL EAAIYARLRS QIVGKVANGG
PNLKKGDNVT DAYLDGLKKS DWFQLRMKDD DAADAIERAQ KQIQAHEKEF EARFADKRGK
ITQGDDLAPG VLKMVKVFLA VKRRIQPGDK MAGRHGNKGV VSNVVPVEDM PYMATGEPVD
IVLNPLGVPS RMNIGQILEV HLGWAAKGLG RKIQRMLEAQ TAVSELRKFL DDIYNHDSAI
NAERVDLSQF SDEELLNLGK NLIDGVPMAT PVFDGASEAE IKRMLELAEL PQSGQTQLYD
GRTGEAFDRK TTVGYMHYLK LNHLVDDKMH ARSTGPYSLV TQQPLGGKAQ FGGQRFGEME
VWALEAYGAA YTLQEMLTVK SDDVQGRNQM YKNIVDGEHE MVAGMPESFN VLVKEIRSLA
INMELEE
