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Sporulation-specific N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) (Autolysin) (Cell wall hydrolase)

 CWLC_BACSU              Reviewed;         255 AA.
Q06320;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 1.
28-MAR-2018, entry version 119.
RecName: Full=Sporulation-specific N-acetylmuramoyl-L-alanine amidase;
EC=3.5.1.28;
AltName: Full=Autolysin;
AltName: Full=Cell wall hydrolase;
Name=cwlC; OrderedLocusNames=BSU17410;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
STRAIN=168;
PubMed=8407798; DOI=10.1128/jb.175.19.6260-6268.1993;
Kuroda A., Asami Y., Sekiguchi J.;
"Molecular cloning of a sporulation-specific cell wall hydrolase gene
of Bacillus subtilis.";
J. Bacteriol. 175:6260-6268(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
SEQUENCE REVISION TO 158.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[4]
PROTEIN SEQUENCE OF 2-11, FUNCTION, CHARACTERIZATION, AND SUBCELLULAR
LOCATION.
STRAIN=168;
PubMed=7601853; DOI=10.1128/jb.177.13.3855-3862.1995;
Smith T.J., Foster S.J.;
"Characterization of the involvement of two compensatory autolysins in
mother cell lysis during sporulation of Bacillus subtilis 168.";
J. Bacteriol. 177:3855-3862(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-255.
STRAIN=168;
Scotti C., Valbuzzi A., Perego M., Galizzi A., Albertini A.M.;
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=10945275; DOI=10.1271/bbb.64.1522;
Shida T., Hattori H., Ise F., Sekiguchi J.;
"Overexpression, purification, and characterization of Bacillus
subtilis N-acetylmuramoyl-L-alanine amidase CwlC.";
Biosci. Biotechnol. Biochem. 64:1522-1525(2000).
[7]
COFACTOR, AND MUTAGENESIS OF HIS-10; GLU-24; ASP-55; HIS-79; ASN-81
AND GLU-141.
PubMed=11375403; DOI=10.1074/jbc.M103903200;
Shida T., Hattori H., Ise F., Sekiguchi J.;
"Mutational analysis of catalytic sites of the cell wall lytic N-
acetylmuramoyl-L-alanine amidases CwlC and CwlV.";
J. Biol. Chem. 276:28140-28146(2001).
[8]
STRUCTURE BY NMR OF 177-255, AND DOMAIN.
PubMed=16042392; DOI=10.1021/bi050624n;
Mishima M., Shida T., Yabuki K., Kato K., Sekiguchi J., Kojima C.;
"Solution structure of the peptidoglycan binding domain of Bacillus
subtilis cell wall lytic enzyme CwlC: characterization of the
sporulation-related repeats by NMR.";
Biochemistry 44:10153-10163(2005).
-!- FUNCTION: Autolysins are involved in some important biological
processes such as cell separation, cell-wall turnover, competence
for genetic transformation, formation of the flagella - in
particular of its basal body - and sporulation. CwlC is able to
hydrolyze type A cell walls such as B.subtilis. Its main function
is to lyze the mother cell wall peptidoglycan, playing a role
during sporulation. {ECO:0000269|PubMed:10945275,
ECO:0000269|PubMed:7601853}.
-!- CATALYTIC ACTIVITY: Hydrolyzes the link between N-acetylmuramoyl
residues and L-amino acid residues in certain cell-wall
glycopeptides.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000305|PubMed:11375403};
-!- ENZYME REGULATION: Inhibited by EDTA.
{ECO:0000269|PubMed:10945275}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 8.5-9.5. {ECO:0000269|PubMed:10945275};
Temperature dependence:
Optimum temperature is 60 degrees Celsius.
{ECO:0000269|PubMed:10945275};
-!- SUBCELLULAR LOCATION: Secreted, cell wall
{ECO:0000269|PubMed:7601853}. Note=Is associated with the mother
cell wall of sporulating cells.
-!- INDUCTION: Induced at 6 to 7 hours after sporulation.
{ECO:0000269|PubMed:8407798}.
-!- DOMAIN: Contains an N-terminal catalytic domain and two C-terminal
tandem repeat sequences that play an important role in
peptidoglycan binding. {ECO:0000269|PubMed:16042392}.
-!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; D14666; BAA03500.1; -; Genomic_DNA.
EMBL; AL009126; CAB13625.2; -; Genomic_DNA.
EMBL; Z68500; CAA92813.1; -; Genomic_DNA.
PIR; A36935; A36935.
RefSeq; NP_389623.2; NC_000964.3.
RefSeq; WP_003244862.1; NZ_JNCM01000035.1.
PDB; 1X60; NMR; -; A=177-255.
PDBsum; 1X60; -.
ProteinModelPortal; Q06320; -.
SMR; Q06320; -.
STRING; 224308.Bsubs1_010100009576; -.
PaxDb; Q06320; -.
EnsemblBacteria; CAB13625; CAB13625; BSU17410.
GeneID; 940088; -.
KEGG; bsu:BSU17410; -.
PATRIC; fig|224308.179.peg.1887; -.
eggNOG; ENOG4105C5C; Bacteria.
eggNOG; COG0860; LUCA.
HOGENOM; HOG000163501; -.
InParanoid; Q06320; -.
KO; K01448; -.
OMA; FKVKANA; -.
PhylomeDB; Q06320; -.
BioCyc; BSUB:BSU17410-MONOMER; -.
EvolutionaryTrace; Q06320; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IBA:GO_Central.
GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
CDD; cd02696; MurNAc-LAA; 1.
Gene3D; 3.30.70.1070; -; 1.
InterPro; IPR002508; MurNAc-LAA_cat.
InterPro; IPR007730; SPOR-like_dom.
InterPro; IPR036680; SPOR-like_sf.
Pfam; PF01520; Amidase_3; 1.
Pfam; PF05036; SPOR; 1.
SMART; SM00646; Ami_3; 1.
SUPFAM; SSF110997; SSF110997; 1.
PROSITE; PS51724; SPOR; 1.
1: Evidence at protein level;
3D-structure; Cell wall; Cell wall biogenesis/degradation; Competence;
Complete proteome; Direct protein sequencing; Hydrolase;
Metal-binding; Reference proteome; Repeat; Secreted; Sporulation;
Zinc.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:7601853}.
CHAIN 2 255 Sporulation-specific N-acetylmuramoyl-L-
alanine amidase.
/FTId=PRO_0000164418.
DOMAIN 180 254 SPOR.
REPEAT 184 219 1.
REPEAT 220 255 2.
REGION 184 255 2 X 35 AA approximate tandem repeats.
ACT_SITE 141 141 {ECO:0000255}.
METAL 10 10 Zinc. {ECO:0000255}.
METAL 24 24 Zinc. {ECO:0000255}.
METAL 79 79 Zinc. {ECO:0000255}.
MUTAGEN 10 10 H->Q: 23% of wild-type activity.
{ECO:0000269|PubMed:11375403}.
MUTAGEN 24 24 E->A,Q,S: Loss of activity.
{ECO:0000269|PubMed:11375403}.
MUTAGEN 55 55 D->V: Loss of activity.
{ECO:0000269|PubMed:11375403}.
MUTAGEN 79 79 H->L: Loss of activity.
{ECO:0000269|PubMed:11375403}.
MUTAGEN 79 79 H->Q: 15% of wild-type activity.
{ECO:0000269|PubMed:11375403}.
MUTAGEN 81 81 N->I: Loss of activity.
{ECO:0000269|PubMed:11375403}.
MUTAGEN 141 141 E->Q,V: Loss of activity.
{ECO:0000269|PubMed:11375403}.
CONFLICT 158 158 S -> T (in Ref. 5; CAA92813).
{ECO:0000305}.
STRAND 185 194 {ECO:0000244|PDB:1X60}.
HELIX 196 209 {ECO:0000244|PDB:1X60}.
STRAND 213 218 {ECO:0000244|PDB:1X60}.
STRAND 221 231 {ECO:0000244|PDB:1X60}.
HELIX 232 245 {ECO:0000244|PDB:1X60}.
STRAND 250 254 {ECO:0000244|PDB:1X60}.
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


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