ID   YKUD_BACLD              Reviewed;         165 AA.
AC   Q65K99; Q62VQ0;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Putative L,D-transpeptidase YkuD;
DE            EC=2.-.-.-;
DE   AltName: Full=Spore protein YkuD homolog;
GN   OrderedLocusNames=BLi01617, BL03652;
OS   Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS   NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=279010;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15383718; DOI=10.1159/000079829;
RA   Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA   Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT   "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT   with great industrial potential.";
RL   J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC   / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX   PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA   Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA   Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA   Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA   Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT   "Complete genome sequence of the industrial bacterium Bacillus
RT   licheniformis and comparisons with closely related Bacillus species.";
RL   Genome Biol. 5:R77.1-R77.12(2004).
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; AE017333; AAU40515.1; -; Genomic_DNA.
DR   EMBL; CP000002; AAU23158.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q65K99; -.
DR   SMR; Q65K99; -.
DR   STRING; 279010.BL03652; -.
DR   MEROPS; C82.003; -.
DR   EnsemblBacteria; AAU23158; AAU23158; BL03652.
DR   KEGG; bld:BLi01617; -.
DR   KEGG; bli:BL03652; -.
DR   eggNOG; COG1376; Bacteria.
DR   HOGENOM; CLU_042399_6_1_9; -.
DR   OMA; FGAYWLS; -.
DR   BioCyc; BLIC279010:BLI_RS08020-MON; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000000606; 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_0000227662"
FT   DOMAIN          2..46
FT                   /note="LysM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
SQ   SEQUENCE   165 AA;  18018 MW;  66ACC28A3B65E92A CRC64;
     MLMYQVKPGE TLESIAADFR TTRQALLQAN PGLNGGQVSA GQSIIIPGIR NPDTIPYRIA
     VSLNGRTLRL YERDRLVKTY PIAVGKILTQ TPRGEFVIVN RQPNPGGPFG AYWLSLSKQH
     YGIHGTNNPS SIGKAVSRGC IRMHNRDVLE LASIVPNGTR VSITP