CWLS_BACSU
ID CWLS_BACSU Reviewed; 414 AA.
AC O31852;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=D-gamma-glutamyl-meso-diaminopimelic acid endopeptidase CwlS;
DE EC=3.4.19.11;
DE AltName: Full=Cell wall lytic enzyme associated with cell separation;
DE Flags: Precursor;
GN Name=cwlS; Synonyms=yojL; OrderedLocusNames=BSU19410;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT the sspC and odhA loci (184 degrees-180 degrees).";
RL DNA Res. 5:195-201(1998).
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 FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=16855244; DOI=10.1128/jb.00188-06;
RA Fukushima T., Afkham A., Kurosawa S., Tanabe T., Yamamoto H., Sekiguchi J.;
RT "A new D,L-endopeptidase gene product, YojL (renamed CwlS), plays a role in
RT cell separation with LytE and LytF in Bacillus subtilis.";
RL J. Bacteriol. 188:5541-5550(2006).
CC -!- FUNCTION: Probably functions as a cell separation enzyme in addition to
CC LytE and LytF. {ECO:0000269|PubMed:16855244}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of gamma-D-glutamyl bonds to the L-terminus
CC (position 7) of meso-diaminopimelic acid (meso-A2pm) in 7-(L-Ala-
CC gamma-D-Glu)-meso-A2pm and 7-(L-Ala-gamma-D-Glu)-7-(D-Ala)-meso-A2pm.
CC It is required that the D-terminal amino and carboxy groups of meso-
CC A2pm are unsubstituted.; EC=3.4.19.11;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6-7 without NaCl at 37 degrees Celsius.
CC {ECO:0000269|PubMed:16855244};
CC Temperature dependence:
CC Optimum temperature is 48 degrees Celsius in 50 mM MOPS-NaOH buffer
CC (pH 7.0) without NaCl. {ECO:0000269|PubMed:16855244};
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:16855244}.
CC Note=Localized at cell separation sites and cell poles during late
CC vegetative phase.
CC -!- DEVELOPMENTAL STAGE: Transcribed during the late vegetative and early
CC stationary phases. {ECO:0000269|PubMed:16855244}.
CC -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC binding.
CC -!- DISRUPTION PHENOTYPE: The cell shape is not significantly different
CC from that of the wild-type. {ECO:0000269|PubMed:16855244}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; AF026147; AAC17860.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13833.1; -; Genomic_DNA.
DR PIR; A69907; A69907.
DR RefSeq; NP_389823.1; NC_000964.3.
DR RefSeq; WP_004399265.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O31852; -.
DR SMR; O31852; -.
DR STRING; 224308.BSU19410; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR MEROPS; C40.008; -.
DR PaxDb; O31852; -.
DR PRIDE; O31852; -.
DR EnsemblBacteria; CAB13833; CAB13833; BSU_19410.
DR GeneID; 939459; -.
DR KEGG; bsu:BSU19410; -.
DR PATRIC; fig|224308.179.peg.2122; -.
DR eggNOG; COG0791; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR InParanoid; O31852; -.
DR OMA; RMITEAK; -.
DR PhylomeDB; O31852; -.
DR BioCyc; BSUB:BSU19410-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008932; F:lytic endotransglycosylase activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 4.
DR Gene3D; 3.10.350.10; -; 4.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF01476; LysM; 4.
DR Pfam; PF00877; NLPC_P60; 1.
DR SMART; SM00257; LysM; 4.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54106; SSF54106; 4.
DR PROSITE; PS51782; LYSM; 4.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 1: Evidence at protein level;
KW Cell wall biogenesis/degradation; Hydrolase; Protease; Reference proteome;
KW Repeat; Signal; Thiol protease.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..414
FT /note="D-gamma-glutamyl-meso-diaminopimelic acid
FT endopeptidase CwlS"
FT /id="PRO_0000019765"
FT DOMAIN 27..70
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 88..131
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 157..200
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 225..268
FT /note="LysM 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 296..414
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT REGION 130..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 201..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 326
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 375
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 387
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ 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
