ID   YKUD_ALKCK              Reviewed;         165 AA.
AC   Q5WC42;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Putative L,D-transpeptidase YkuD;
DE            EC=2.-.-.-;
DE   AltName: Full=Spore protein YkuD homolog;
GN   OrderedLocusNames=ABC3535;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Probable enzyme that may play an important role in cell wall
CC       biology. {ECO:0000250}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Spore wall {ECO:0000250}. Note=Probably localized
CC       either on the surface of the outer spore membrane and/or in the inner
CC       spore coat. {ECO:0000250}.
CC   -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC       binding.
CC   -!- SIMILARITY: Belongs to the YkuD family. {ECO:0000305}.
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DR   EMBL; AP006627; BAD66068.1; -; Genomic_DNA.
DR   RefSeq; WP_011248373.1; NC_006582.1.
DR   AlphaFoldDB; Q5WC42; -.
DR   SMR; Q5WC42; -.
DR   STRING; 66692.ABC3535; -.
DR   MEROPS; C82.003; -.
DR   EnsemblBacteria; BAD66068; BAD66068; ABC3535.
DR   KEGG; bcl:ABC3535; -.
DR   eggNOG; COG1376; Bacteria.
DR   HOGENOM; CLU_042399_6_1_9; -.
DR   OMA; FGAYWLS; -.
DR   OrthoDB; 975147at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000001168; Chromosome.
DR   GO; GO:0031160; C:spore wall; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 1.
DR   CDD; cd16913; YkuD_like; 1.
DR   Gene3D; 2.40.440.10; -; 1.
DR   Gene3D; 3.10.350.10; -; 1.
DR   InterPro; IPR005490; LD_TPept_cat_dom.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR038063; Transpep_catalytic_dom.
DR   Pfam; PF01476; LysM; 1.
DR   Pfam; PF03734; YkuD; 1.
DR   SMART; SM00257; LysM; 1.
DR   SUPFAM; SSF141523; SSF141523; 1.
DR   SUPFAM; SSF54106; SSF54106; 1.
DR   PROSITE; PS51782; LYSM; 1.
PE   3: Inferred from homology;
KW   Cell shape; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Hydrolase; Peptidoglycan synthesis; Reference proteome; Sporulation;
KW   Transferase.
FT   CHAIN           1..165
FT                   /note="Putative L,D-transpeptidase YkuD"
FT                   /id="PRO_0000227663"
FT   DOMAIN          2..46
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
SQ   SEQUENCE   165 AA;  17896 MW;  389B5F9B4F97D4B5 CRC64;
     MFFHSVQQGE TLSSIAADYR ISLSHLIQAN PTINPNQLFV GQSIVIPGLP NPNTIPYEIH
     VSLSQHQLTL LHNGSVVKIY PIAVGKMLTQ TPTGNFVIVN KAPNPGGPFG TMWMSLSKLH
     YGIHGTNDPS SIGKSVSHGC IRMHNKDVEE LAATVPIGTR VRIEP