ID   CWLA_BACSU              Reviewed;         272 AA.
AC   P24808;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   27-MAR-2024, entry version 146.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase CwlA;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
GN   Name=cwlA; OrderedLocusNames=BSU25900;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC   STRAIN=168;
RX   PubMed=2127796; DOI=10.1099/00221287-136-11-2209;
RA   Kuroda A., Sekiguchi J.;
RT   "Cloning, sequencing and genetic mapping of a Bacillus subtilis cell wall
RT   hydrolase gene.";
RL   J. Gen. Microbiol. 136:2209-2216(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1683402; DOI=10.1099/00221287-137-8-1987;
RA   Foster S.J.;
RT   "Cloning, expression, sequence analysis and biochemical characterization of
RT   an autolytic amidase of Bacillus subtilis 168 trpC2.";
RL   J. Gen. Microbiol. 137:1987-1998(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=7704261; DOI=10.1099/13500872-141-2-323;
RA   Takemaru K., Mizuno M., Sato T., Takeuchi M., Kobayashi Y.;
RT   "Complete nucleotide sequence of a skin element excised by DNA
RT   rearrangement during sporulation in Bacillus subtilis.";
RL   Microbiology 141:323-327(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [5]
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).
CC   -!- FUNCTION: Autolysins are involved in some important biological
CC       processes such as cell separation, cell-wall turnover, competence for
CC       genetic transformation, formation of the flagella and sporulation.
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   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; X51424; CAA35788.1; -; Genomic_DNA.
DR   EMBL; M59232; AAA62676.1; -; Genomic_DNA.
DR   EMBL; D32216; BAA06960.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12424.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14531.1; -; Genomic_DNA.
DR   PIR; S26671; C44816.
DR   RefSeq; NP_390467.1; NC_000964.3.
DR   RefSeq; WP_003229946.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P24808; -.
DR   SMR; P24808; -.
DR   STRING; 224308.BSU25900; -.
DR   PaxDb; 224308-BSU25900; -.
DR   EnsemblBacteria; CAB14531; CAB14531; BSU_25900.
DR   GeneID; 937772; -.
DR   KEGG; bsu:BSU25900; -.
DR   PATRIC; fig|224308.179.peg.2815; -.
DR   eggNOG; COG3409; Bacteria.
DR   eggNOG; COG5632; Bacteria.
DR   InParanoid; P24808; -.
DR   OrthoDB; 9794294at2; -.
DR   PhylomeDB; P24808; -.
DR   BioCyc; BSUB:BSU25900-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IBA:GO_Central.
DR   GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd06583; PGRP; 1.
DR   Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR   Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR   InterPro; IPR036505; Amidase/PGRP_sf.
DR   InterPro; IPR002502; Amidase_domain.
DR   InterPro; IPR002477; Peptidoglycan-bd-like.
DR   InterPro; IPR036365; PGBD-like_sf.
DR   InterPro; IPR036366; PGBDSf.
DR   PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR   PANTHER; PTHR30417:SF11; N-ACETYLMURAMOYL-L-ALANINE AMIDASE XLYA; 1.
DR   Pfam; PF01510; Amidase_2; 1.
DR   Pfam; PF01471; PG_binding_1; 1.
DR   SMART; SM00644; Ami_2; 1.
DR   SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR   SUPFAM; SSF47090; PGBD-like; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Competence; Direct protein sequencing;
KW   Hydrolase; Reference proteome; Sporulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:2127796"
FT   CHAIN           2..272
FT                   /note="N-acetylmuramoyl-L-alanine amidase CwlA"
FT                   /id="PRO_0000006453"
FT   DOMAIN          24..142
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   272 AA;  29958 MW;  43B2AB1ADC1F5DFA CRC64;
     MAIKVVKNLV SKSKYGLKCP NPMKAEYITI HNTANDASAA NEISYMKNNS SSTSFHFAVD
     DKQVIQGIPT NRNAWHTGDG TNGTGNRKSI GVEICYSKSG GVRYKAAEKL AIKFVAQLLK
     ERGWGIDRVR KHQDWNGKYC PHRILSEGRW IQVKTAIEAE LKKLGGKTNS SKASVAKKKT
     TNTSSKKTSY ALPSGIFKVK SPMMRGEKVT QIQKALAALY FYPDKGAKNN GIDGVYGPKT
     ADAIRRFQSM YGLTQDGIYG PKTKAKLEAL LK
//