CWLK_BACSU
ID CWLK_BACSU Reviewed; 167 AA.
AC O34360; Q797R8;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Peptidoglycan L-alanyl-D-glutamate endopeptidase CwlK;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN Name=cwlK; Synonyms=ycdD; OrderedLocusNames=BSU02810;
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=9274031; DOI=10.1099/00221287-143-8-2775;
RA Kumano M., Tamakoshi A., Yamane K.;
RT "A 32 kb nucleotide sequence from the region of the lincomycin-resistance
RT gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and
RT identification of the site of the lin-2 mutation.";
RL Microbiology 143:2775-2782(1997).
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 CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION,
RP AND EXPRESSION.
RC STRAIN=168;
RX PubMed=17588176; DOI=10.1007/s00438-007-0255-8;
RA Fukushima T., Yao Y., Kitajima T., Yamamoto H., Sekiguchi J.;
RT "Characterization of new L,D-endopeptidase gene product CwlK (previous
RT YcdD) that hydrolyzes peptidoglycan in Bacillus subtilis.";
RL Mol. Genet. Genomics 278:371-383(2007).
CC -!- FUNCTION: Cleaves the linkage of the L-alanine-D-glutamic acid of
CC B.subtilis cell wall.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:17588176};
CC Temperature dependence:
CC Optimum temperature is 37 degrees Celsius.
CC {ECO:0000269|PubMed:17588176};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17588176}.
CC -!- DEVELOPMENTAL STAGE: Expressed during vegetative growth phase.
CC -!- SIMILARITY: Belongs to the peptidase M15C family. {ECO:0000305}.
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DR EMBL; AB000617; BAA22242.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12075.1; -; Genomic_DNA.
DR PIR; F69755; F69755.
DR RefSeq; NP_388163.1; NC_000964.3.
DR RefSeq; WP_009966473.1; NZ_JNCM01000030.1.
DR AlphaFoldDB; O34360; -.
DR SMR; O34360; -.
DR STRING; 224308.BSU02810; -.
DR MEROPS; M15.A05; -.
DR PaxDb; O34360; -.
DR EnsemblBacteria; CAB12075; CAB12075; BSU_02810.
DR GeneID; 938378; -.
DR KEGG; bsu:BSU02810; -.
DR PATRIC; fig|224308.179.peg.292; -.
DR eggNOG; COG1876; Bacteria.
DR OMA; YIRHEWH; -.
DR PhylomeDB; O34360; -.
DR BioCyc; BSUB:BSU02810-MON; -.
DR BRENDA; 3.4.24.B24; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1380.10; -; 1.
DR InterPro; IPR009045; Hedgehog_sig/DD-Pept_Zn-bd_sf.
DR InterPro; IPR039561; Peptidase_M15C.
DR Pfam; PF13539; Peptidase_M15_4; 1.
DR SUPFAM; SSF55166; SSF55166; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell wall biogenesis/degradation; Hydrolase; Membrane;
KW Reference proteome; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..167
FT /note="Peptidoglycan L-alanyl-D-glutamate endopeptidase
FT CwlK"
FT /id="PRO_0000297706"
SQ SEQUENCE 167 AA; 19113 MW; 1724607AA1769905 CRC64;
MNLPAKTFVI LCILFLLDLC FSYIRHEWHS QNALQDMPVP SDLHPIVKQN ADALKAAAAN
KGIDVVITEG FRSFKEQDEL YKQGRTKKGN IVTYARGGES YHNYGLAIDF ALQKKDGSII
WDMEYDGNQN GKSDWLEVVE IAKTLGFEWG GDWKRFKDYP HLEMIPN
