ID   YRAA_BACSU              Reviewed;         169 AA.
AC   O06006;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   24-OCT-2003, sequence version 2.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Putative cysteine protease YraA;
DE            EC=3.2.-.-;
GN   Name=yraA; OrderedLocusNames=BSU27020;
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=9141695; DOI=10.1099/00221287-143-4-1321;
RA   Parro V., San Roman M., Galindo I., Purnelle B., Bolotin A., Sorokin A.,
RA   Mellado R.P.;
RT   "A 23911 bp region of the Bacillus subtilis genome comprising genes located
RT   upstream and downstream of the lev operon.";
RL   Microbiology 143:1321-1326(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 C-TERMINUS.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [4]
RP   INDUCTION.
RC   STRAIN=168 / 1604;
RX   PubMed=17434969; DOI=10.1128/jb.00130-07;
RA   Jervis A.J., Thackray P.D., Houston C.W., Horsburgh M.J., Moir A.;
RT   "SigM-responsive genes of Bacillus subtilis and their promoters.";
RL   J. Bacteriol. 189:4534-4538(2007).
RN   [5]
RP   FUNCTION, INDUCTION, OPERON STRUCTURE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=168;
RX   PubMed=19170879; DOI=10.1111/j.1365-2958.2008.06568.x;
RA   Nguyen T.T.H., Eiamphungporn W., Maeder U., Liebeke M., Lalk M., Hecker M.,
RA   Helmann J.D., Antelmann H.;
RT   "Genome-wide responses to carbonyl electrophiles in Bacillus subtilis:
RT   control of the thiol-dependent formaldehyde dehydrogenase AdhA and cysteine
RT   proteinase YraA by the MerR-family regulator YraB (AdhR).";
RL   Mol. Microbiol. 71:876-894(2009).
CC   -!- FUNCTION: Functions in the protection against aldehyde-stress, possibly
CC       by degrading damaged proteins. {ECO:0000269|PubMed:19170879}.
CC   -!- INDUCTION: The adhR-yraA operon is induced by formaldehyde and
CC       methylgloxal, under the control of AdhR (PubMed:19170879). A second
CC       yraA-specific transcription unit is not induced by formaldehyde or
CC       methylglyoxal and is not controlled by AdhR (PubMed:19170879).
CC       Transcribed under partial control of SigM ECF sigma factor
CC       (PubMed:17434969). {ECO:0000269|PubMed:19170879}.
CC   -!- DISRUPTION PHENOTYPE: No aldehyde-stress related phenotype; when
CC       combined with a yfkM disruption shows significantly reduced growth in
CC       the presence of formaldehye and methylglyoxal.
CC       {ECO:0000269|PubMed:19170879}.
CC   -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA63466.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X92868; CAA63466.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL009126; CAB14644.2; -; Genomic_DNA.
DR   PIR; A69970; A69970.
DR   RefSeq; NP_390580.2; NC_000964.3.
DR   RefSeq; WP_003229836.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; O06006; -.
DR   SMR; O06006; -.
DR   STRING; 224308.BSU27020; -.
DR   MEROPS; C56.001; -.
DR   jPOST; O06006; -.
DR   PaxDb; O06006; -.
DR   PRIDE; O06006; -.
DR   EnsemblBacteria; CAB14644; CAB14644; BSU_27020.
DR   GeneID; 937603; -.
DR   KEGG; bsu:BSU27020; -.
DR   PATRIC; fig|224308.179.peg.2935; -.
DR   eggNOG; COG0693; Bacteria.
DR   InParanoid; O06006; -.
DR   OMA; LCHGPWV; -.
DR   PhylomeDB; O06006; -.
DR   BioCyc; BSUB:BSU27020-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR006286; C56_PfpI.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR002818; DJ-1/PfpI.
DR   PANTHER; PTHR42733; PTHR42733; 1.
DR   Pfam; PF01965; DJ-1_PfpI; 1.
DR   SUPFAM; SSF52317; SSF52317; 1.
DR   TIGRFAMs; TIGR01382; PfpI; 1.
DR   PROSITE; PS51276; PEPTIDASE_C56_PFPI; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Reference proteome; Stress response.
FT   CHAIN           1..169
FT                   /note="Putative cysteine protease YraA"
FT                   /id="PRO_0000157833"
FT   DOMAIN          3..169
FT                   /note="PfpI endopeptidase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT   ACT_SITE        103
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00608"
SQ   SEQUENCE   169 AA;  18512 MW;  1AB077EC1536BE71 CRC64;
     MSKKIAVLVT DQFEDIEYTS PVKAYEEAGY SVVAIDLEAG KEVTGKHGEK VKIDKAISDV
     DASDFDALLI PGGFSPDLLR ADDRPGEFAK AFVENKKPVF AICHGPQVLI DTDLLKGKDI
     TGYRSIRKDL INAGANYKDA EVVVSHNIVT SRTPDDLEAF NRESLNLLK