ID   RHGT2_BACSU             Reviewed;         217 AA.
AC   O31528;
DT   03-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Probable rhamnogalacturonan acetylesterase YesY;
DE            Short=RGAE;
DE            EC=3.1.1.-;
GN   Name=yesY; OrderedLocusNames=BSU07070;
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   FUNCTION IN DEGRADATION OF TYPE I RHAMNOGALACTURONAN, AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=17449691; DOI=10.1128/aem.00147-07;
RA   Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT   "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT   clusters responsible for rhamnogalacturonan depolymerization.";
RL   Appl. Environ. Microbiol. 73:3803-3813(2007).
CC   -!- FUNCTION: May play a role in the degradation of rhamnogalacturonan
CC       derived from plant cell walls. Probably has broad substrate specificity
CC       and may degrade several types of acetylated substrates.
CC       {ECO:0000269|PubMed:17449691}.
CC   -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC       {ECO:0000269|PubMed:17449691}.
CC   -!- SIMILARITY: Belongs to the 'GDSL' lipolytic enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; AL009126; CAB12526.1; -; Genomic_DNA.
DR   PIR; H69797; H69797.
DR   RefSeq; NP_388588.1; NC_000964.3.
DR   RefSeq; WP_003244014.1; NZ_CP053102.1.
DR   AlphaFoldDB; O31528; -.
DR   SMR; O31528; -.
DR   STRING; 224308.BSU07070; -.
DR   PaxDb; O31528; -.
DR   PRIDE; O31528; -.
DR   EnsemblBacteria; CAB12526; CAB12526; BSU_07070.
DR   GeneID; 938772; -.
DR   KEGG; bsu:BSU07070; -.
DR   PATRIC; fig|224308.179.peg.767; -.
DR   eggNOG; COG2755; Bacteria.
DR   InParanoid; O31528; -.
DR   OMA; QMGHNDA; -.
DR   PhylomeDB; O31528; -.
DR   BioCyc; BSUB:BSU07070-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   CDD; cd01821; Rhamnogalacturan_acetylesterase_like; 1.
DR   Gene3D; 3.40.50.1110; -; 1.
DR   InterPro; IPR001087; GDSL.
DR   InterPro; IPR037459; RhgT-like.
DR   InterPro; IPR036514; SGNH_hydro_sf.
DR   PANTHER; PTHR43695; PTHR43695; 1.
DR   Pfam; PF00657; Lipase_GDSL; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..217
FT                   /note="Probable rhamnogalacturonan acetylesterase YesY"
FT                   /id="PRO_0000364433"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        178
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        185
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   217 AA;  24594 MW;  7FF4EC62C4C473F2 CRC64;
     MANHIYLAGD STVQTYGDST NQGGWGQFLG SHLPEHIQVI NRAIGGRSSK TFVEEGRLQA
     ILDVIEPDDW LFVQMGHNDA SKNKPERYTE PYTTYKQYLK QYIAGAREKG AHPLLITPVA
     RFHYENGVFL NDFPDYCIAM KQTAAEENVQ LIDLMEKSLA FFTEKGEEKV YTYFMISEGI
     NDYTHFTKKG ANEMAKLVAK GIKELGLPLT ESIIKER