YYDH_BACSU
ID YYDH_BACSU Reviewed; 252 AA.
AC Q45594; Q794X1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Putative peptide zinc metalloprotease protein YydH;
GN Name=yydH; OrderedLocusNames=BSU40160;
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=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(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 SEQUENCE REVISION TO 9.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP TRANSCRIPTION REGULATION, AND OPERON SUGGESTION.
RC STRAIN=168;
RX PubMed=15743949; DOI=10.1128/jb.187.6.2010-2019.2005;
RA Albano M., Smits W.K., Ho L.T., Kraigher B., Mandic-Mulec I., Kuipers O.P.,
RA Dubnau D.;
RT "The Rok protein of Bacillus subtilis represses genes for cell surface and
RT extracellular functions.";
RL J. Bacteriol. 187:2010-2019(2005).
RN [5]
RP SUGGESTION OF FUNCTION, AND OPERON STRUCTURE.
RC STRAIN=168;
RX PubMed=17921301; DOI=10.1128/jb.01181-07;
RA Butcher B.G., Lin Y.-P., Helmann J.D.;
RT "The yydFGHIJ operon of Bacillus subtilis encodes a peptide that induces
RT the LiaRS two-component system.";
RL J. Bacteriol. 189:8616-8625(2007).
CC -!- FUNCTION: Required for production of the modified peptide YydF
CC (Probable). May process the precursor form of YydF to release the
CC active peptide (Potential). {ECO:0000305}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Transcriptionally repressed by rok.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; D78193; BAA11274.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16053.2; -; Genomic_DNA.
DR PIR; F70091; F70091.
DR RefSeq; NP_391896.2; NC_000964.3.
DR RefSeq; WP_003243055.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; Q45594; -.
DR STRING; 224308.BSU40160; -.
DR MEROPS; M50.A09; -.
DR PaxDb; Q45594; -.
DR PRIDE; Q45594; -.
DR EnsemblBacteria; CAB16053; CAB16053; BSU_40160.
DR GeneID; 937745; -.
DR KEGG; bsu:BSU40160; -.
DR PATRIC; fig|224308.179.peg.4344; -.
DR eggNOG; COG1994; Bacteria.
DR OMA; YFIMNIV; -.
DR BioCyc; BSUB:BSU40160-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Hydrolase; Membrane; Metal-binding; Metalloprotease;
KW Protease; Reference proteome; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..252
FT /note="Putative peptide zinc metalloprotease protein YydH"
FT /id="PRO_0000370195"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 231..251
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 106
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT CONFLICT 9
FT /note="E -> G (in Ref. 1; BAA11274)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 252 AA; 29942 MW; A31FCE4CE7EF04D9 CRC64;
MKILKYEDEK YEVLVQNNVF IKDKKSGEYY KNSLNSLSDK QLLRFKMYKE KVSPKFFYLF
LSFTALMFIL NYIHLIKLQN GLSSVFYGWK MWIIIVIYFI MNIVLHELGH IYSLKFFGKN
FDKVGFKLNF YVFPAFYVQL NETYMLSRNE KIIVHLFGLF INYLLINTLE LINQFTFSSE
ALTMAFMLFS STLLWNLIPI LNSDGYKILL AFLSLDEYSR FKTNHWLVLT IQIIGIGLAV
NSVVHWILYI VN
