ID   YISK_BACSU              Reviewed;         301 AA.
AC   O06724; Q796R1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Uncharacterized protein YisK;
GN   Name=yisK; OrderedLocusNames=BSU10750;
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=9353931; DOI=10.1099/00221287-143-10-3305;
RA   Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J.;
RT   "Sequencing of regions downstream of addA (98 degrees) and citG (289
RT   degrees) in Bacillus subtilis.";
RL   Microbiology 143:3305-3308(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   INDUCTION BY NUTRIENT LIMITATION CONDITIONS.
RC   STRAIN=168;
RX   PubMed=16847875; DOI=10.1002/pmic.200600100;
RA   Tam L.T., Antelmann H., Eymann C., Albrecht D., Bernhardt J., Hecker M.;
RT   "Proteome signatures for stress and starvation in Bacillus subtilis as
RT   revealed by a 2-D gel image color coding approach.";
RL   Proteomics 6:4565-4585(2006).
CC   -!- INDUCTION: In response to ammonium, tryptophan, glucose, and phosphate
CC       starvation. {ECO:0000269|PubMed:16847875}.
CC   -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y09476; CAA70682.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12915.1; -; Genomic_DNA.
DR   PIR; C69837; C69837.
DR   RefSeq; NP_388956.1; NC_000964.3.
DR   RefSeq; WP_003245441.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O06724; -.
DR   SMR; O06724; -.
DR   STRING; 224308.BSU10750; -.
DR   jPOST; O06724; -.
DR   PaxDb; O06724; -.
DR   PRIDE; O06724; -.
DR   EnsemblBacteria; CAB12915; CAB12915; BSU_10750.
DR   GeneID; 936356; -.
DR   KEGG; bsu:BSU10750; -.
DR   PATRIC; fig|224308.179.peg.1156; -.
DR   eggNOG; COG0179; Bacteria.
DR   InParanoid; O06724; -.
DR   OMA; YALSIDM; -.
DR   PhylomeDB; O06724; -.
DR   BioCyc; BSUB:BSU10750-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0018773; F:acetylpyruvate hydrolase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.850.10; -; 1.
DR   InterPro; IPR011234; Fumarylacetoacetase-like_C.
DR   InterPro; IPR036663; Fumarylacetoacetase_C_sf.
DR   Pfam; PF01557; FAA_hydrolase; 1.
DR   SUPFAM; SSF56529; SSF56529; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Reference proteome.
FT   CHAIN           1..301
FT                   /note="Uncharacterized protein YisK"
FT                   /id="PRO_0000383352"
FT   BINDING         148
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         150
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
FT   BINDING         179
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  33146 MW;  D97C68F9577A864B CRC64;
     MKFATGELYN RMFVGLIIDD EKIMDLQKAE KKLFELETIP GSLIECIAEG DKFVAHARQL
     AEWAKKPNDE LGSFMYSLSE VKLHAPIPKP SKNIICIGKN YRDHAIEMGS EADIPEHPMV
     FTKSPVTVTG HGDIVKSHEE VTSQLDYEGE LAVVIGKSGT RISKEDAYDH VFGYTIVNDI
     TARDLQKRHK QFFIGKSLDT TCPMGPVLVH KSSIQEPERL KVETRVNGEL RQSGSASDMI
     FSIPELIETL SKGMTLEAGD IIATGTPSGV GKGFTPPKFL RSGDKIDITI DPIGTLSNQI
     G