CWLC_BACSU
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 03-AUG-2022, entry version 135.
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; Firmicutes; 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; Q06320; -.
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 OMA; FESYIYP; -.
DR PhylomeDB; Q06320; -.
DR BioCyc; BSUB:BSU17410-MON; -.
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; -; 1.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR007730; SPOR-like_dom.
DR InterPro; IPR036680; SPOR-like_sf.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF05036; SPOR; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF110997; SSF110997; 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
