ID   YABG_BACSU              Reviewed;         290 AA.
AC   P37548;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=Sporulation-specific protease YabG;
DE            EC=3.4.-.-;
GN   Name=yabG; OrderedLocusNames=BSU00430;
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=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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   FUNCTION.
RC   STRAIN=168;
RX   PubMed=11040425; DOI=10.1111/j.1574-6968.2000.tb09355.x;
RA   Takamatsu H., Imamura A., Kodama T., Asai K., Ogasawara N., Watabe K.;
RT   "The yabG gene of Bacillus subtilis encodes a sporulation specific protease
RT   which is involved in the processing of several spore coat proteins.";
RL   FEMS Microbiol. Lett. 192:33-38(2000).
RN   [4]
RP   SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND TRANSCRIPTION.
RC   STRAIN=168;
RX   PubMed=10714992; DOI=10.1128/jb.182.7.1883-1888.2000;
RA   Takamatsu H., Kodama T., Imamura A., Asai K., Kobayashi K., Nakayama T.,
RA   Ogasawara N., Watabe K.;
RT   "The Bacillus subtilis yabG gene is transcribed by SigK RNA polymerase
RT   during sporulation, and yabG mutant spores have altered coat protein
RT   composition.";
RL   J. Bacteriol. 182:1883-1888(2000).
RN   [5]
RP   POSSIBLE ROLE IN CROSS-LINKING OF GERQ, AND DISRUPTION PHENOTYPE.
RX   PubMed=16751597; DOI=10.1093/jb/mvj096;
RA   Kuwana R., Okuda N., Takamatsu H., Watabe K.;
RT   "Modification of GerQ reveals a functional relationship between Tgl and
RT   YabG in the coat of Bacillus subtilis spores.";
RL   J. Biochem. 139:887-901(2006).
CC   -!- FUNCTION: Cleaves the spore coat proteins SpoIVA and SafA. May
CC       cooperate with tgl to mediate the temperature-dependent cross-linking
CC       of coat proteins like GerQ. {ECO:0000269|PubMed:11040425}.
CC   -!- SUBCELLULAR LOCATION: Forespore outer membrane
CC       {ECO:0000269|PubMed:10714992}. Note=Synthesized in the mother cell
CC       compartment and assembled on the surface of the forespore.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the mother cell compartment from T4
CC       of sporulation.
CC   -!- INDUCTION: Induced by SigK.
CC   -!- DISRUPTION PHENOTYPE: According to PubMed:10714992, cells have an
CC       altered coat protein composition; CotT, YeeK, YxeE, CotF, SafA and
CC       SpoIVA proteins are present at increased levels and/or exist as
CC       precursors. According to PubMed:16751597, cells show no effects on
CC       vegetative growth or spore resistance to heat, chloroform or lysozyme.
CC       The germination of YabG mutant spores in L-alanine and in a mixture of
CC       L-asparagine, D-glucose, D-fructose and potassium chloride was the same
CC       as that of the wild-type spores. Heat treatment for 20 minutes at 60
CC       degrees Celsius, which maximally activates the Tgl enzymatic activity,
CC       causes cross-linking of GerQ in isolated YabG-deleted spores but not in
CC       Tgl/YabG double-mutant spores. Additionally, the germination frequency
CC       of the Tgl/YabG double-mutant spores in the presence of L-alanine with
CC       or without heat activation at 60 degrees Celsius is lower than that of
CC       wild-type spores. {ECO:0000269|PubMed:10714992,
CC       ECO:0000269|PubMed:16751597}.
CC   -!- SIMILARITY: Belongs to the peptidase U57 family. {ECO:0000305}.
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DR   EMBL; D26185; BAA05278.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11819.1; -; Genomic_DNA.
DR   PIR; S66072; S66072.
DR   RefSeq; NP_387924.1; NC_000964.3.
DR   RefSeq; WP_003243478.1; NZ_JNCM01000028.1.
DR   AlphaFoldDB; P37548; -.
DR   SMR; P37548; -.
DR   STRING; 224308.BSU00430; -.
DR   MEROPS; U57.001; -.
DR   PaxDb; P37548; -.
DR   PRIDE; P37548; -.
DR   EnsemblBacteria; CAB11819; CAB11819; BSU_00430.
DR   GeneID; 937005; -.
DR   KEGG; bsu:BSU00430; -.
DR   PATRIC; fig|224308.179.peg.43; -.
DR   eggNOG; ENOG502Z7P7; Bacteria.
DR   OMA; MPGKVLH; -.
DR   PhylomeDB; P37548; -.
DR   BioCyc; BSUB:BSU00430-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0043593; C:endospore coat; IMP:CACAO.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   InterPro; IPR008764; Peptidase_U57.
DR   Pfam; PF05582; Peptidase_U57; 1.
DR   PIRSF; PIRSF011575; YabG; 1.
DR   TIGRFAMs; TIGR02855; spore_yabG; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Membrane; Reference proteome; Sporulation.
FT   CHAIN           1..290
FT                   /note="Sporulation-specific protease YabG"
FT                   /id="PRO_0000049441"
SQ   SEQUENCE   290 AA;  33318 MW;  B60A5B9F9D3209BB CRC64;
     MQFQIGDMVA RKSYQMDVLF RIIGIEQTSK GNSIAILHGD EVRLIADSDF SDLVAVKKDE
     QMMRKKKDES RMNESLELLR QDYKLLREKQ EYYATSQYQH QEHYFHMPGK VLHLDGDEAY
     LKKCLNVYKK IGVPVYGIHC HEKKMSASIE VLLDKYRPDI LVITGHDAYS KQKGGIDDLN
     AYRHSKHFVE TVQTARKKIP HLDQLVIFAG ACQSHFESLI RAGANFASSP SRVNIHALDP
     VYIVAKISFT PFMERINVWE VLRNTLTREK GLGGIETRGV LRIGMPYKSN