ID   CWLH_BACSU              Reviewed;         250 AA.
AC   P54450;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase CwlH;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
DE   Flags: Precursor;
GN   Name=cwlH; Synonyms=yqeE; OrderedLocusNames=BSU25710;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
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   [2]
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   [3]
RP   CHARACTERIZATION.
RC   STRAIN=168;
RX   PubMed=10515909; DOI=10.1128/jb.181.20.6230-6237.1999;
RA   Nugroho F.A., Yamamoto H., Kobayashi Y., Sekiguchi J.;
RT   "Characterization of a new sigma-K-dependent peptidoglycan hydrolase gene
RT   that plays a role in Bacillus subtilis mother cell lysis.";
RL   J. Bacteriol. 181:6230-6237(1999).
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       Could play a role in mother cell lysis with CwlC.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.0.;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during the late sporulation phase.
CC   -!- INDUCTION: Expression is GerE and sigma K-dependent.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC       {ECO:0000305}.
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DR   EMBL; D84432; BAA12441.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14512.1; -; Genomic_DNA.
DR   PIR; A69951; A69951.
DR   RefSeq; NP_390448.1; NC_000964.3.
DR   RefSeq; WP_003229963.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P54450; -.
DR   SMR; P54450; -.
DR   STRING; 224308.BSU25710; -.
DR   PaxDb; 224308-BSU25710; -.
DR   EnsemblBacteria; CAB14512; CAB14512; BSU_25710.
DR   GeneID; 937808; -.
DR   KEGG; bsu:BSU25710; -.
DR   PATRIC; fig|224308.179.peg.2796; -.
DR   eggNOG; COG3409; Bacteria.
DR   eggNOG; COG5632; Bacteria.
DR   InParanoid; P54450; -.
DR   OrthoDB; 9794294at2; -.
DR   PhylomeDB; P54450; -.
DR   BioCyc; BSUB:BSU25710-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; 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; Hydrolase;
KW   Reference proteome; Secreted; Signal; Sporulation.
FT   SIGNAL          1..44
FT                   /evidence="ECO:0000255"
FT   CHAIN           45..250
FT                   /note="N-acetylmuramoyl-L-alanine amidase CwlH"
FT                   /id="PRO_0000006454"
FT   DOMAIN          45..141
FT                   /note="N-acetylmuramoyl-L-alanine amidase"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   250 AA;  27571 MW;  E88E0AAD66533FC2 CRC64;
     MVTIKKDFIP VSNDNRPGYA MAPAYITVHN TANTAKGADA KMHAKFVKNP NTSESWHFTV
     DDSVIYQHLP IDENGWHAGD GTNGTGNRKS IGIEICENAD GDFEKATSNA QWLIRKLMKE
     NNIPLNRVVP HKKWSGKECP RKLLDHWNSF LNGISSSDTP PKETSPSYPL PSGVIKLTSP
     YRKGTNILQL QKALAVLHFY PDKGAKNNGI DGVYGPKTAN AVKRFQLMNG LTADGIYGPK
     TKAKLKSKLK
//