ID   YNGK_BACSU              Reviewed;         510 AA.
AC   O35015; Q799L9;
DT   07-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Glycosyl hydrolase YngK {ECO:0000250|UniProtKB:P64426};
DE            EC=3.2.1.- {ECO:0000250|UniProtKB:P64426};
DE   Flags: Precursor;
GN   Name=yngK; Synonyms=yotA; OrderedLocusNames=BSU18280;
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=9387222; DOI=10.1099/00221287-143-11-3443;
RA   Tosato V., Albertini A.M., Zotti M., Sonda S., Bruschi C.V.;
RT   "Sequence completion, identification and definition of the fengycin operon
RT   in Bacillus subtilis 168.";
RL   Microbiology 143:3443-3450(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   DISRUPTION PHENOTYPE.
RC   STRAIN=168 / CU1065;
RX   PubMed=10960106; DOI=10.1128/jb.182.18.5202-5210.2000;
RA   Turner M.S., Helmann J.D.;
RT   "Mutations in multidrug efflux homologs, sugar isomerases, and
RT   antimicrobial biosynthesis genes differentially elevate activity of the
RT   sigma(X) and sigma(W) factors in Bacillus subtilis.";
RL   J. Bacteriol. 182:5202-5210(2000).
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene show up-regulated sigma X
CC       activity. {ECO:0000269|PubMed:10960106}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase-like 10 (GHL10) family.
CC       {ECO:0000305}.
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DR   EMBL; Y13917; CAA74215.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13711.1; -; Genomic_DNA.
DR   PIR; H69893; H69893.
DR   RefSeq; NP_389710.1; NC_000964.3.
DR   RefSeq; WP_003231519.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O35015; -.
DR   SMR; O35015; -.
DR   STRING; 224308.BSU18280; -.
DR   PaxDb; O35015; -.
DR   PRIDE; O35015; -.
DR   EnsemblBacteria; CAB13711; CAB13711; BSU_18280.
DR   GeneID; 939977; -.
DR   KEGG; bsu:BSU18280; -.
DR   PATRIC; fig|224308.179.peg.1995; -.
DR   eggNOG; COG1649; Bacteria.
DR   InParanoid; O35015; -.
DR   OMA; YGPWSEY; -.
DR   PhylomeDB; O35015; -.
DR   BioCyc; BSUB:BSU18280-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR003790; GHL10.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF02638; GHL10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Glycosidase; Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..510
FT                   /note="Glycosyl hydrolase YngK"
FT                   /id="PRO_0000379126"
SQ   SEQUENCE   510 AA;  58868 MW;  51C4280436D2937F CRC64;
     MKVCQKSIVR FLVSLIIGTF VISVPFMANA QSDRELRAVW IASVLNIDWP SKKGLSVKEQ
     KQEYIKLLDD VQKMGMNAVI VQIKPTADAF YPSAYGPWSE YLTGVQGKDP GYDPLAFMIE
     ETHKRNLEFH AWFNPYRITM NHTDLNKLSE DHPARKHPDW VAAYGNQLYY HPGIPEARDF
     IVKGIEEVVK HYDIDAVHMD DYFYPYKIAG QEFPDQAQYE QYGKDAFSNI DDWRRDNVNQ
     LVKQINQTIK AAKPYVKFGI SPFGVWRNAA DDPTGSNTKA GVRNYDDLYA DTRHWIQEGD
     IDYIAPQIYW SIGFNAAAYD VLADWWSNEV KNRPVHLYIG QAAYKINNNF DPPWSDPEEY
     VRQITLNRQL ELVKGSMHFS LKDLNKNPLG IKDSLSTDLY SKPALVPQMP WLDNTAPKKP
     KLTKVTEDKN GNLLQIKDHP SNQKTKETAY YAIYRAEGKK QRTLLATQRK THEQQTFLDN
     TADPNKKYTY YVTSADRLHN ESKASKRTTK