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D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS (EC 3.4.19.11) (Cell wall lytic enzyme associated with cell separation)

 CWLS_BACSU              Reviewed;         414 AA.
O31852;
16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
25-OCT-2017, entry version 113.
RecName: Full=D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS;
EC=3.4.19.11;
AltName: Full=Cell wall lytic enzyme associated with cell separation;
Flags: Precursor;
Name=cwlS; Synonyms=yojL; OrderedLocusNames=BSU19410;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
PubMed=9734814; DOI=10.1093/dnares/5.3.195;
Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A.,
Ehrlich S.D., Park S.-H.;
"Sequence analysis of the Bacillus subtilis 168 chromosome region
between the sspC and odhA loci (184 degrees-180 degrees).";
DNA Res. 5:195-201(1998).
[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]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
STRAIN=168;
PubMed=16855244; DOI=10.1128/JB.00188-06;
Fukushima T., Afkham A., Kurosawa S., Tanabe T., Yamamoto H.,
Sekiguchi J.;
"A new D,L-endopeptidase gene product, YojL (renamed CwlS), plays a
role in cell separation with LytE and LytF in Bacillus subtilis.";
J. Bacteriol. 188:5541-5550(2006).
-!- FUNCTION: Probably functions as a cell separation enzyme in
addition to LytE and LytF. {ECO:0000269|PubMed:16855244}.
-!- CATALYTIC ACTIVITY: Hydrolysis of gamma-D-glutamyl bonds to the L-
terminus (position 7) of meso-diaminopimelic acid (meso-A(2)pm) in
7-(L-Ala-gamma-D-Glu)-meso-A(2)pm and 7-(L-Ala-gamma-D-Glu)-7-(D-
Ala)-meso-A(2)pm. It is required that the D-terminal amino and
carboxy groups of meso-A(2)pm are unsubstituted.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 6-7 without NaCl at 37 degrees Celsius.
{ECO:0000269|PubMed:16855244};
Temperature dependence:
Optimum temperature is 48 degrees Celsius in 50 mM MOPS-NaOH
buffer (pH 7.0) without NaCl. {ECO:0000269|PubMed:16855244};
-!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16855244}.
Note=Localized at cell separation sites and cell poles during late
vegetative phase.
-!- DEVELOPMENTAL STAGE: Transcribed during the late vegetative and
early stationary phases. {ECO:0000269|PubMed:16855244}.
-!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
binding.
-!- DISRUPTION PHENOTYPE: The cell shape is not significantly
different from that of the wild-type.
{ECO:0000269|PubMed:16855244}.
-!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF026147; AAC17860.1; -; Genomic_DNA.
EMBL; AL009126; CAB13833.1; -; Genomic_DNA.
PIR; A69907; A69907.
RefSeq; NP_389823.1; NC_000964.3.
RefSeq; WP_004399265.1; NZ_JNCM01000036.1.
ProteinModelPortal; O31852; -.
SMR; O31852; -.
STRING; 224308.Bsubs1_010100010716; -.
CAZy; CBM50; Carbohydrate-Binding Module Family 50.
MEROPS; C40.008; -.
PaxDb; O31852; -.
EnsemblBacteria; CAB13833; CAB13833; BSU19410.
GeneID; 939459; -.
KEGG; bsu:BSU19410; -.
PATRIC; fig|224308.179.peg.2122; -.
eggNOG; ENOG4105K4H; Bacteria.
eggNOG; COG0791; LUCA.
eggNOG; COG1388; LUCA.
HOGENOM; HOG000229978; -.
InParanoid; O31852; -.
KO; K19220; -.
OMA; RMITEAK; -.
PhylomeDB; O31852; -.
BioCyc; BSUB:BSU19410-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
CDD; cd00118; LysM; 4.
Gene3D; 3.10.350.10; -; 4.
InterPro; IPR018392; LysM_dom.
InterPro; IPR036779; LysM_dom_sf.
InterPro; IPR000064; NLP_P60_dom.
Pfam; PF01476; LysM; 4.
Pfam; PF00877; NLPC_P60; 1.
SMART; SM00257; LysM; 4.
SUPFAM; SSF54106; SSF54106; 4.
PROSITE; PS51782; LYSM; 4.
1: Evidence at protein level;
Cell wall biogenesis/degradation; Complete proteome; Hydrolase;
Protease; Reference proteome; Repeat; Signal; Thiol protease.
SIGNAL 1 26 {ECO:0000255}.
CHAIN 27 414 D-gamma-glutamyl-meso-diaminopimelic acid
endopeptidase CwlS.
/FTId=PRO_0000019765.
DOMAIN 27 70 LysM 1. {ECO:0000255|PROSITE-
ProRule:PRU01118}.
DOMAIN 88 131 LysM 2. {ECO:0000255|PROSITE-
ProRule:PRU01118}.
DOMAIN 157 200 LysM 3. {ECO:0000255|PROSITE-
ProRule:PRU01118}.
DOMAIN 225 268 LysM 4. {ECO:0000255|PROSITE-
ProRule:PRU01118}.
COMPBIAS 135 140 Poly-Ser.
ACT_SITE 326 326 Nucleophile. {ECO:0000250}.
ACT_SITE 375 375 Proton acceptor. {ECO:0000250}.
SEQUENCE 414 AA; 44235 MW; 25C5B188221B2F87 CRC64;
MKKKIVAGLA VSAVVGSSMA AAPAEAKTIK VKSGDSLWKL SRQYDTTISA LKSENKLKST
VLYVGQSLKV PESSKKSTTS PSNSSKTSTY TVAYGDSLWM IAKNHKMSVS ELKSLNSLSS
DLIRPGQKLK IKGTSSSSGS NGSKKNSGSN SSGSSKSTYT VKLGDSLWKI ANSLNMTVAE
LKTLNGLTSD TLYPKQVLKI KGSSSPKNGN SGSKKPSNSN PSKTTTYKVK AGDSLWKIAN
RLGVTVQSIR DKNNLSSDVL QIGQVLTISG ASKSNPSNPT KPTKPKDNSG SNIQIGSKID
RMITEAKKYV GVPYRWGGNT PAGFDCSGFI YYLINNVSSI SRLSTAGYWN VMQKVSQPSV
GDFVFFTTYK SGPSHMGIYL GGGDFIHASS SGVDISNLSN SYWKQRYLGA RSYF


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