RPOY_BACSU
ID RPOY_BACSU Reviewed; 69 AA.
AC O31718;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=DNA-directed RNA polymerase subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01553, ECO:0000303|PubMed:25092033};
DE Short=RNAP epsilon subunit {ECO:0000255|HAMAP-Rule:MF_01553};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01553, ECO:0000269|PubMed:6802805};
DE AltName: Full=DNA-directed RNA polymerase subunit omega 1 {ECO:0000303|PubMed:18289874};
DE AltName: Full=RNA polymerase epsilon subunit {ECO:0000255|HAMAP-Rule:MF_01553};
DE AltName: Full=RNA polymerase omega 1 subunit {ECO:0000303|PubMed:6802805};
DE AltName: Full=Transcriptase subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01553};
DE AltName: Full=Transcriptase subunit omega 1 {ECO:0000305};
GN Name=rpoY {ECO:0000255|HAMAP-Rule:MF_01553, ECO:0000303|PubMed:25092033};
GN Synonyms=ykzG; OrderedLocusNames=BSU14540;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=6802805; DOI=10.1128/jb.150.2.977-980.1982;
RA Achberger E.C., Tahara M., Whiteley H.R.;
RT "Interchangeability of delta subunits of RNA polymerase from different
RT species of the genus Bacillus.";
RL J. Bacteriol. 150:977-980(1982).
RN [3]
RP SUBUNIT, AND IDENTIFICATION.
RC STRAIN=BS200;
RX PubMed=18289874; DOI=10.1016/j.pep.2008.01.006;
RA Yang X., Lewis P.J.;
RT "Overproduction and purification of recombinant Bacillus subtilis RNA
RT polymerase.";
RL Protein Expr. Purif. 59:86-93(2008).
RN [4]
RP SUBUNIT.
RC STRAIN=168;
RX PubMed=21710567; DOI=10.1002/pmic.201000790;
RA Delumeau O., Lecointe F., Muntel J., Guillot A., Guedon E., Monnet V.,
RA Hecker M., Becher D., Polard P., Noirot P.;
RT "The dynamic protein partnership of RNA polymerase in Bacillus subtilis.";
RL Proteomics 11:2992-3001(2011).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE,
RP AND MUTAGENESIS OF ARG-34; 41-LYS--VAL-50; 46-PHE--THR-48 AND
RP 61-SER--LEU-69.
RC STRAIN=168 / BSB1;
RX PubMed=25092033; DOI=10.1128/jb.02020-14;
RA Keller A.N., Yang X., Wiedermannova J., Delumeau O., Krasny L., Lewis P.J.;
RT "epsilon, a new subunit of RNA polymerase found in gram-positive
RT bacteria.";
RL J. Bacteriol. 196:3622-3632(2014).
CC -!- FUNCTION: A non-essential component of RNA polymerase (RNAP)
CC (PubMed:6802805, PubMed:18289874, PubMed:21710567, PubMed:25092033).
CC Has a similar structure to bacteriophage T7 protein Gp2 (AC P03704),
CC which is known to bind to RNAP in the DNA binding-cleft. Unlike Gp2
CC however, this protein does not inhibit transcription initiation
CC (PubMed:25092033). In vitro reconstitution experiments show this
CC subunit is dispensible (PubMed:18289874). {ECO:0000269|PubMed:18289874,
CC ECO:0000269|PubMed:21710567, ECO:0000269|PubMed:25092033,
CC ECO:0000269|PubMed:6802805}.
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_01553};
CC -!- SUBUNIT: Monomer (By similarity). RNAP is composed of a core of 2
CC alpha, a beta and a beta' subunit. The core is associated with a delta
CC subunit, and at least one of epsilon or omega (PubMed:6802805,
CC PubMed:18289874, PubMed:21710567, PubMed:25092033). When a sigma factor
CC is associated with the core the holoenzyme is formed, which can
CC initiate transcription (PubMed:18289874).
CC {ECO:0000250|UniProtKB:A0A0K2H5X8, ECO:0000269|PubMed:18289874,
CC ECO:0000269|PubMed:21710567, ECO:0000269|PubMed:25092033,
CC ECO:0000269|PubMed:6802805}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000269|PubMed:25092033}. Note=Colocalizes with RNAP.
CC {ECO:0000269|PubMed:25092033}.
CC -!- INDUCTION: Part of the rpoY-rnjA operon, transcribed constitutively.
CC {ECO:0000269|PubMed:25092033}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype; growth, bacterial fitness
CC in competition experiments, RNAP distribution, global transcript levels
CC and transcription initiation in vitro are all unaffected.
CC {ECO:0000269|PubMed:25092033}.
CC -!- SIMILARITY: Belongs to the RNA polymerase subunit epsilon family.
CC {ECO:0000255|HAMAP-Rule:MF_01553}.
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DR EMBL; AL009126; CAB13327.1; -; Genomic_DNA.
DR PIR; D69871; D69871.
DR RefSeq; NP_389337.1; NC_000964.3.
DR RefSeq; WP_003222303.1; NZ_JNCM01000035.1.
DR PDB; 6WVK; EM; 3.36 A; E=1-69.
DR PDB; 6ZCA; EM; 4.20 A; E=1-69.
DR PDB; 6ZFB; EM; 3.90 A; E/e=1-69.
DR PDB; 7CKQ; EM; 4.40 A; H=1-69.
DR PDB; 7F75; EM; 4.20 A; H=1-69.
DR PDBsum; 6WVK; -.
DR PDBsum; 6ZCA; -.
DR PDBsum; 6ZFB; -.
DR PDBsum; 7CKQ; -.
DR PDBsum; 7F75; -.
DR AlphaFoldDB; O31718; -.
DR SMR; O31718; -.
DR STRING; 224308.BSU14540; -.
DR jPOST; O31718; -.
DR PaxDb; O31718; -.
DR PRIDE; O31718; -.
DR EnsemblBacteria; CAB13327; CAB13327; BSU_14540.
DR GeneID; 64303342; -.
DR GeneID; 939482; -.
DR KEGG; bsu:BSU14540; -.
DR PATRIC; fig|224308.179.peg.1584; -.
DR eggNOG; COG5503; Bacteria.
DR OMA; TIYVEGE; -.
DR PhylomeDB; O31718; -.
DR BioCyc; BSUB:BSU14540-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
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:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01553; RNApol_bact_RpoY; 1.
DR InterPro; IPR009907; RpoY.
DR Pfam; PF07288; RpoY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA-directed RNA polymerase;
KW Nucleotidyltransferase; Reference proteome; Transcription; Transferase.
FT CHAIN 1..69
FT /note="DNA-directed RNA polymerase subunit epsilon"
FT /id="PRO_0000163121"
FT MUTAGEN 34
FT /note="R->A: No change in subcellular localization."
FT /evidence="ECO:0000269|PubMed:25092033"
FT MUTAGEN 41..50
FT /note="KFNIEFITPV->AAAAAAAAAA: No longer localizes to the
FT nucleoid."
FT /evidence="ECO:0000269|PubMed:25092033"
FT MUTAGEN 46..48
FT /note="FIT->AAA: No change in subcellular localization."
FT /evidence="ECO:0000269|PubMed:25092033"
FT MUTAGEN 61..69
FT /note="SENFKVLEL->AAAAAAAAA: No change in subcellular
FT localization."
FT /evidence="ECO:0000269|PubMed:25092033"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 21..26
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 30..36
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:6WVK"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:6WVK"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:6WVK"
SQ SEQUENCE 69 AA; 8252 MW; 4A6F31075B01943D CRC64;
MIYKVFYQEK ADEVPVREKT DSLYIEGVSE RDVRTKLKEK KFNIEFITPV DGAFLEYEQQ
SENFKVLEL
