LYTH_BACSU
ID LYTH_BACSU Reviewed; 326 AA.
AC O32130;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=L-Ala--D-Glu endopeptidase;
DE EC=3.4.-.-;
DE AltName: Full=Peptidoglycan hydrolase;
DE AltName: Full=Sporulation-specific endopeptidase;
DE Flags: Precursor;
GN Name=lytH; Synonyms=yunA, yutA; OrderedLocusNames=BSU32340;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
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 [2]
RP FUNCTION, AND TRANSCRIPTIONAL REGULATION.
RC STRAIN=168;
RX PubMed=12813075; DOI=10.1128/jb.185.13.3813-3820.2003;
RA Horsburgh G.J., Atrih A., Foster S.J.;
RT "Characterization of LytH, a differentiation-associated peptidoglycan
RT hydrolase of Bacillus subtilis involved in endospore cortex maturation.";
RL J. Bacteriol. 185:3813-3820(2003).
CC -!- FUNCTION: L-Ala--D-Glu endopeptidase involved in production of single
CC L-alanine side chains from tetrapeptides in the spore cortex
CC peptidoglycan. Therefore, is required for the endospore cortex
CC maturation. {ECO:0000269|PubMed:12813075}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- DEVELOPMENTAL STAGE: Expressed only during sporulation.
CC -!- INDUCTION: Expressed under the control of the late mother cell-specific
CC sigma factor sigma-K. {ECO:0000269|PubMed:12813075}.
CC -!- MISCELLANEOUS: The presence of single L-alanine residues in the spore
CC cortex increases the spores ability to be resistant to heat.
CC -!- SIMILARITY: Belongs to the peptidase M23B family. {ECO:0000305}.
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DR EMBL; AL009126; CAB15224.2; -; Genomic_DNA.
DR PIR; D70015; D70015.
DR RefSeq; NP_391114.2; NC_000964.3.
DR RefSeq; WP_003243462.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; O32130; -.
DR SMR; O32130; -.
DR STRING; 224308.BSU32340; -.
DR MEROPS; M23.010; -.
DR PaxDb; O32130; -.
DR PRIDE; O32130; -.
DR EnsemblBacteria; CAB15224; CAB15224; BSU_32340.
DR GeneID; 936510; -.
DR KEGG; bsu:BSU32340; -.
DR PATRIC; fig|224308.179.peg.3501; -.
DR eggNOG; COG0739; Bacteria.
DR OMA; WSFDPYP; -.
DR BioCyc; BSUB:BSU32340-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.70.70.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell wall biogenesis/degradation; Differentiation; Hydrolase;
KW Metal-binding; Metalloprotease; Protease; Reference proteome; Signal;
KW Sporulation; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..326
FT /note="L-Ala--D-Glu endopeptidase"
FT /id="PRO_0000165904"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 292
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
SQ SEQUENCE 326 AA; 36957 MW; 4E7DE2A55D3F7534 CRC64;
MKVLLSALLL LLFAFEPSAS GKKLSDPVLS KRMELYHKIE AVTQIPWYAL AAVDQYEENV
RSNRKDLPEK AGIISIYIPD DIWSGPENPN PKDDAPLSIK VFDGIGMDGD GDGKAEVSND
EDILYTFSQY LLSYGTDEDN IRIGLWNYYR RDQTVGIISE FMKLFKAYGH IDLGEHAFPL
PIRTDYSYRS TWGDARGFGG RRIHEGTDIF AHYGLPVKST CYGVVEMKGW NRFGGWRIGI
RDINNTYHYF AHLNGFAKGI KTGQIVEPGQ VIGSVGSSGY GPPGTAGKFP PHLHYGMYKD
NGRTEWSFDP YPHLRAWERY EYQKKK
