(data stored in ACNUC7421 zone)

SWISSPROT: CWLD_BACSU

ID   CWLD_BACSU              Reviewed;         237 AA.
AC   P50864;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   11-DEC-2019, entry version 117.
DE   RecName: Full=Germination-specific N-acetylmuramoyl-L-alanine amidase;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
DE   Flags: Precursor;
GN   Name=cwlD; OrderedLocusNames=BSU01530;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7559346; DOI=10.1128/jb.177.19.5582-5589.1995;
RA   Sekiguchi J., Akeo K., Yamamoto H., Khasanov F.K., Alonso J.C., Kuroda A.;
RT   "Nucleotide sequence and regulation of a new putative cell wall hydrolase
RT   gene, cwlD, which affects germination in Bacillus subtilis.";
RL   J. Bacteriol. 177:5582-5589(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969501; DOI=10.1099/13500872-142-11-3039;
RA   Yasumoto K., Liu H., Jeong S.M., Ohashi Y., Kakinuma S., Tanaka K.,
RA   Kawamura F., Yoshikawa H., Takahashi H.;
RT   "Sequence analysis of a 50 kb region between spo0H and rrnH on the Bacillus
RT   subtilis chromosome.";
RL   Microbiology 142:3039-3046(1996).
RN   [3]
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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=14679227; DOI=10.1128/jb.186.1.80-89.2004;
RA   Gilmore M.E., Bandyopadhyay D., Dean A.M., Linnstaedt S.D., Popham D.L.;
RT   "Production of muramic delta-lactam in Bacillus subtilis spore
RT   peptidoglycan.";
RL   J. Bacteriol. 186:80-89(2004).
CC   -!- FUNCTION: Cleaves the peptide side chain from the N-acetylmuramic acid
CC       residues in peptidoglycan. This is a step in the formation of muramic
CC       delta-lactam residues in spore cortex. {ECO:0000269|PubMed:14679227}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC         amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC         Evidence={ECO:0000269|PubMed:14679227};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expression of cwlD takes place in both the mother
CC       cell and forespore compartments of sporulating cells.
CC       {ECO:0000269|PubMed:14679227}.
CC   -!- MISCELLANEOUS: CwlD and PdaA are necessary and sufficient for muramic
CC       delta-lactam production in B.subtilis spore peptidoglycan.
CC       {ECO:0000305|PubMed:14679227}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
DR   EMBL; X74737; CAA52758.1; -; Genomic_DNA.
DR   EMBL; D64126; BAA10993.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11929.1; -; Genomic_DNA.
DR   PIR; G69610; G69610.
DR   RefSeq; NP_388034.1; NC_000964.3.
DR   RefSeq; WP_004399672.1; NZ_JNCM01000029.1.
DR   SMR; P50864; -.
DR   STRING; 224308.BSU01530; -.
DR   PaxDb; P50864; -.
DR   PRIDE; P50864; -.
DR   DNASU; 938917; -.
DR   EnsemblBacteria; CAB11929; CAB11929; BSU01530.
DR   GeneID; 938917; -.
DR   KEGG; bsu:BSU01530; -.
DR   PATRIC; fig|224308.179.peg.157; -.
DR   eggNOG; COG0860; LUCA.
DR   HOGENOM; HOG000163501; -.
DR   InParanoid; P50864; -.
DR   KO; K01448; -.
DR   OMA; QIRPVHH; -.
DR   PhylomeDB; P50864; -.
DR   BioCyc; BSUB:BSU01530-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR014234; Spore_CwlD.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   TIGRFAMs; TIGR02883; spore_cwlD; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P50864.
DR   SWISS-2DPAGE; P50864.
KW   Cell wall biogenesis/degradation; Hydrolase; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..237
FT                   /note="Germination-specific N-acetylmuramoyl-L-alanine
FT                   amidase"
FT                   /id="PRO_0000164419"
FT   DOMAIN          43..226
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   237 AA;  27006 MW;  E5B92E58552B59D6 CRC64;
     MRKKLKWLSF LLGFIILLFL FKYQFSNNDS WKPWSLPLSG KIIYLDPGHG GPDGGAVGGK
     LLEKDVTLEV AFRVRDYLQE QGALVIMTRE SDTDLAPEGT KGYSRRKAED LRQRVKLINH
     SEAELYISIH LNAIPSQKWS GAQSFYYGKY AENEKVAKYI QDELRRNLEN TTRKAKRIHG
     IYLMQNVTKP GALIEVGFLS NPSEATLLGK PKYQDKVASS IYKGILRYFT EKGDPPE
//

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