YTNP_BACSU
ID YTNP_BACSU Reviewed; 281 AA.
AC O34760; Q795S8;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable quorum-quenching lactonase YtnP;
DE EC=3.1.1.-;
GN Name=ytnP; OrderedLocusNames=BSU29890;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
RN [2]
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=168;
RX PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA Mann M.;
RT "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT Bacillus subtilis.";
RL Mol. Cell. Proteomics 6:697-707(2007).
RN [4]
RP FUNCTION, INDUCTION, AND MUTAGENESIS OF SER-36.
RX PubMed=22101040; DOI=10.1128/aem.06992-11;
RA Schneider J., Yepes A., Garcia-Betancur J.C., Westedt I., Mielich B.,
RA Lopez D.;
RT "Streptomycin-induced expression in Bacillus subtilis of YtnP, a lactonase-
RT homologous protein that inhibits development and streptomycin production in
RT Streptomyces griseus.";
RL Appl. Environ. Microbiol. 78:599-603(2012).
CC -!- FUNCTION: Probable hydrolase that is able to inhibit the signaling
CC pathway required for the streptomycin production and development of
CC aerial mycelium in S.griseus. Thus, serves as a defensive strategy
CC against competing bacteria. The putative target for YtnP may be a
CC gamma-butyrolactone termed A factor, which is the quorum-sensing
CC signaling molecule that positively regulates streptomycin production
CC and development of aerial hyphae in S.griseus.
CC {ECO:0000269|PubMed:22101040}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- INDUCTION: By the antimicrobial streptomycin, produced by the Gram-
CC positive bacterium S.griseus. {ECO:0000269|PubMed:22101040}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00286.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAB14967.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF008220; AAC00286.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB14967.1; ALT_INIT; Genomic_DNA.
DR PIR; G69997; G69997.
DR RefSeq; NP_390867.1; NC_000964.3.
DR RefSeq; WP_003246020.1; NZ_CP053102.1.
DR RefSeq; WP_010886594.1; NC_000964.3.
DR AlphaFoldDB; O34760; -.
DR SMR; O34760; -.
DR STRING; 224308.BSU29890; -.
DR iPTMnet; O34760; -.
DR PaxDb; O34760; -.
DR PRIDE; O34760; -.
DR EnsemblBacteria; CAB14967; CAB14967; BSU_29890.
DR GeneID; 937981; -.
DR KEGG; bsu:BSU29890; -.
DR PATRIC; fig|224308.179.peg.3247; -.
DR eggNOG; COG0491; Bacteria.
DR InParanoid; O34760; -.
DR BioCyc; BSUB:BSU29890-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.60.15.10; -; 1.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..281
FT /note="Probable quorum-quenching lactonase YtnP"
FT /id="PRO_0000361998"
FT BINDING 111
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 113
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17218307"
FT MUTAGEN 36
FT /note="S->A: Does not abrogate the development of aerial
FT mycelium in S.griseus."
FT /evidence="ECO:0000269|PubMed:22101040"
SQ SEQUENCE 281 AA; 31801 MW; 858479A5A5A97FCE CRC64;
METMKIGNIT LTWLDGGVTH MDGGAMFGVV PKPLWSKKYP VNEKNQIELR TDPILIQKDG
LNIIIDAGIG YGKLTDKQKR NYGVTQESNV KPSLAALGLT VADIDVIAMT HLHFDHACGL
TEYEGERLVS VFPNAVIYTS AVEWDEMRHP NIRSKNTYWK ENWEAVAGQV KTFEDTLTIT
EGITMHHTGG HSDGHSVLIC EDAGETAVHM ADLMPTHAHR NPLWVLAYDD YPMTSIPQKQ
KWQAFAAEKD AWFIFYHDAE YRALQWEEDG SIKKSVKRMK R
