RPOB_XANCP
ID RPOB_XANCP Reviewed; 1387 AA.
AC Q8PC56; Q8RTJ8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=XCC0888;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Wang Z.-R., Wang T.-Y., Yang M.-T.;
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL74153.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008922; AAM40198.1; -; Genomic_DNA.
DR EMBL; AF426390; AAL74153.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_636274.1; NC_003902.1.
DR AlphaFoldDB; Q8PC56; -.
DR SMR; Q8PC56; -.
DR STRING; 340.xcc-b100_3466; -.
DR EnsemblBacteria; AAM40198; AAM40198; XCC0888.
DR KEGG; xcc:XCC0888; -.
DR PATRIC; fig|190485.4.peg.959; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_6; -.
DR OMA; FMTWEGY; -.
DR BRENDA; 2.7.7.6; 6708.
DR Proteomes; UP000001010; 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; Reference proteome;
KW Transcription; Transferase.
FT CHAIN 1..1387
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_0000047999"
FT CONFLICT 155
FT /note="F -> V (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="G -> A (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 344
FT /note="G -> A (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="V -> S (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 677..678
FT /note="KP -> NA (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 696
FT /note="A -> P (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 1073
FT /note="R -> P (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 1105
FT /note="I -> V (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 1110
FT /note="K -> N (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 1185..1186
FT /note="EL -> DV (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
FT CONFLICT 1326
FT /note="A -> R (in Ref. 2; AAL74153)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1387 AA; 154903 MW; E650928EBD3B3375 CRC64;
MEDLMTSYSF TEKKRIRKDF GKQRSILEVP FLLAIQVDSY REFLQEDVEP NKRKDLGLHA
ALKSVFPISS YSGNAALEYV GYKLGEPVFD ERECRQRGMS YGAPLRVTVR LVIYDRESST
KAIKYVKEQE VYLGEIPLMT ENGTFIVNGT ERVIFSQLHR 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
