ID   CWLC_BACSU              Reviewed;         255 AA.
AC   Q06320;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   27-MAR-2024, entry version 141.
DE   RecName: Full=Sporulation-specific N-acetylmuramoyl-L-alanine amidase;
DE            EC=3.5.1.28;
DE   AltName: Full=Autolysin;
DE   AltName: Full=Cell wall hydrolase;
GN   Name=cwlC; OrderedLocusNames=BSU17410;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=168;
RX   PubMed=8407798; DOI=10.1128/jb.175.19.6260-6268.1993;
RA   Kuroda A., Asami Y., Sekiguchi J.;
RT   "Molecular cloning of a sporulation-specific cell wall hydrolase gene of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 175:6260-6268(1993).
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   SEQUENCE REVISION TO 158.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-11, FUNCTION, CHARACTERIZATION, AND SUBCELLULAR
RP   LOCATION.
RC   STRAIN=168;
RX   PubMed=7601853; DOI=10.1128/jb.177.13.3855-3862.1995;
RA   Smith T.J., Foster S.J.;
RT   "Characterization of the involvement of two compensatory autolysins in
RT   mother cell lysis during sporulation of Bacillus subtilis 168.";
RL   J. Bacteriol. 177:3855-3862(1995).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-255.
RC   STRAIN=168;
RA   Scotti C., Valbuzzi A., Perego M., Galizzi A., Albertini A.M.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX   PubMed=10945275; DOI=10.1271/bbb.64.1522;
RA   Shida T., Hattori H., Ise F., Sekiguchi J.;
RT   "Overexpression, purification, and characterization of Bacillus subtilis N-
RT   acetylmuramoyl-L-alanine amidase CwlC.";
RL   Biosci. Biotechnol. Biochem. 64:1522-1525(2000).
RN   [7]
RP   COFACTOR, AND MUTAGENESIS OF HIS-10; GLU-24; ASP-55; HIS-79; ASN-81 AND
RP   GLU-141.
RX   PubMed=11375403; DOI=10.1074/jbc.m103903200;
RA   Shida T., Hattori H., Ise F., Sekiguchi J.;
RT   "Mutational analysis of catalytic sites of the cell wall lytic N-
RT   acetylmuramoyl-L-alanine amidases CwlC and CwlV.";
RL   J. Biol. Chem. 276:28140-28146(2001).
RN   [8]
RP   STRUCTURE BY NMR OF 177-255, AND DOMAIN.
RX   PubMed=16042392; DOI=10.1021/bi050624n;
RA   Mishima M., Shida T., Yabuki K., Kato K., Sekiguchi J., Kojima C.;
RT   "Solution structure of the peptidoglycan binding domain of Bacillus
RT   subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-
RT   related repeats by NMR.";
RL   Biochemistry 44:10153-10163(2005).
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 - in particular of
CC       its basal body - and sporulation. CwlC is able to hydrolyze type A cell
CC       walls such as B.subtilis. Its main function is to lyze the mother cell
CC       wall peptidoglycan, playing a role during sporulation.
CC       {ECO:0000269|PubMed:10945275, ECO:0000269|PubMed:7601853}.
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   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000305|PubMed:11375403};
CC   -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:10945275}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 8.5-9.5. {ECO:0000269|PubMed:10945275};
CC       Temperature dependence:
CC         Optimum temperature is 60 degrees Celsius.
CC         {ECO:0000269|PubMed:10945275};
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:7601853}.
CC       Note=Is associated with the mother cell wall of sporulating cells.
CC   -!- INDUCTION: Induced at 6 to 7 hours after sporulation.
CC       {ECO:0000269|PubMed:8407798}.
CC   -!- DOMAIN: Contains an N-terminal catalytic domain and two C-terminal
CC       tandem repeat sequences that play an important role in peptidoglycan
CC       binding. {ECO:0000269|PubMed:16042392}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; D14666; BAA03500.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13625.2; -; Genomic_DNA.
DR   EMBL; Z68500; CAA92813.1; -; Genomic_DNA.
DR   PIR; A36935; A36935.
DR   RefSeq; NP_389623.2; NC_000964.3.
DR   RefSeq; WP_003244862.1; NZ_JNCM01000035.1.
DR   PDB; 1X60; NMR; -; A=177-255.
DR   PDBsum; 1X60; -.
DR   AlphaFoldDB; Q06320; -.
DR   BMRB; Q06320; -.
DR   SMR; Q06320; -.
DR   STRING; 224308.BSU17410; -.
DR   PaxDb; 224308-BSU17410; -.
DR   EnsemblBacteria; CAB13625; CAB13625; BSU_17410.
DR   GeneID; 940088; -.
DR   KEGG; bsu:BSU17410; -.
DR   PATRIC; fig|224308.179.peg.1887; -.
DR   eggNOG; COG0860; Bacteria.
DR   InParanoid; Q06320; -.
DR   OrthoDB; 9763643at2; -.
DR   PhylomeDB; Q06320; -.
DR   BioCyc; BSUB:BSU17410-MONOMER; -.
DR   EvolutionaryTrace; Q06320; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
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; IEA:InterPro.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd02696; MurNAc-LAA; 1.
DR   Gene3D; 3.30.70.1070; Sporulation related repeat; 1.
DR   Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR   InterPro; IPR002508; MurNAc-LAA_cat.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   InterPro; IPR036680; SPOR-like_sf.
DR   PANTHER; PTHR30404:SF5; AUTOLYSIN PH-RELATED; 1.
DR   PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR   Pfam; PF01520; Amidase_3; 1.
DR   Pfam; PF05036; SPOR; 1.
DR   SMART; SM00646; Ami_3; 1.
DR   SUPFAM; SSF110997; Sporulation related repeat; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell wall; Cell wall biogenesis/degradation; Competence;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Reference proteome;
KW   Repeat; Secreted; Sporulation; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:7601853"
FT   CHAIN           2..255
FT                   /note="Sporulation-specific N-acetylmuramoyl-L-alanine
FT                   amidase"
FT                   /id="PRO_0000164418"
FT   DOMAIN          4..172
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          180..254
FT                   /note="SPOR"
FT   REPEAT          184..219
FT                   /note="1"
FT   REPEAT          220..255
FT                   /note="2"
FT   REGION          184..255
FT                   /note="2 X 35 AA approximate tandem repeats"
FT   ACT_SITE        141
FT                   /evidence="ECO:0000255"
FT   BINDING         10
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         79
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   MUTAGEN         10
FT                   /note="H->Q: 23% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:11375403"
FT   MUTAGEN         24
FT                   /note="E->A,Q,S: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11375403"
FT   MUTAGEN         55
FT                   /note="D->V: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11375403"
FT   MUTAGEN         79
FT                   /note="H->L: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11375403"
FT   MUTAGEN         79
FT                   /note="H->Q: 15% of wild-type activity."
FT                   /evidence="ECO:0000269|PubMed:11375403"
FT   MUTAGEN         81
FT                   /note="N->I: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11375403"
FT   MUTAGEN         141
FT                   /note="E->Q,V: Loss of activity."
FT                   /evidence="ECO:0000269|PubMed:11375403"
FT   CONFLICT        158
FT                   /note="S -> T (in Ref. 5; CAA92813)"
FT                   /evidence="ECO:0000305"
FT   STRAND          185..194
FT                   /evidence="ECO:0007829|PDB:1X60"
FT   HELIX           196..209
FT                   /evidence="ECO:0007829|PDB:1X60"
FT   STRAND          213..218
FT                   /evidence="ECO:0007829|PDB:1X60"
FT   STRAND          221..231
FT                   /evidence="ECO:0007829|PDB:1X60"
FT   HELIX           232..245
FT                   /evidence="ECO:0007829|PDB:1X60"
FT   STRAND          250..254
FT                   /evidence="ECO:0007829|PDB:1X60"
SQ   SEQUENCE   255 AA;  27146 MW;  30C950116784FBC1 CRC64;
     MVKIFIDPGH GGSDPGATGN GLQEKTLTLQ IALALRTILT NEYEGVSLLL SRTSDQYVSL
     NDRTNAANNW GADFFLSIHV NSGGGTGFES YIYPDVGAPT TTYQSTIHSE VIQAVDFADR
     GKKTANFHVL RESAMPALLT ENGFIDTVSD ANKLKTSSFI QSLARGHANG LEQAFNLKKT
     SSSGLYKVQI GAFKVKANAD SLASNAEAKG FDSIVLLKDG LYKVQIGAFS SKDNADTLAA
     RAKNAGFDAI VILES
//