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Peptidoglycan DL-endopeptidase CwlO (EC 3.4.-.-) (D-gamma-glutamyl-meso-diaminopimelyl DL-endopeptidase) (PSPA2)

 CWLO_BACSU              Reviewed;         473 AA.
P40767; O06969;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
30-MAY-2000, sequence version 2.
07-NOV-2018, entry version 111.
RecName: Full=Peptidoglycan DL-endopeptidase CwlO;
EC=3.4.-.-;
AltName: Full=D-gamma-glutamyl-meso-diaminopimelyl DL-endopeptidase;
AltName: Full=PSPA2;
Flags: Precursor;
Name=cwlO; Synonyms=yvcE, yzkA; OrderedLocusNames=BSU34800;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=168;
Denizot F.;
Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
[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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
PubMed=3145906; DOI=10.1016/0378-1119(88)90207-7;
Smith H., de Jong A., Bron S., Venema G.;
"Characterization of signal-sequence-coding regions selected from the
Bacillus subtilis chromosome.";
Gene 70:351-361(1988).
[4]
ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=168;
PubMed=11987133;
DOI=10.1002/1615-9861(200205)2:5<591::AID-PROT591>3.0.CO;2-8;
Antelmann H., Yamamoto H., Sekiguchi J., Hecker M.;
"Stabilization of cell wall proteins in Bacillus subtilis: a proteomic
approach.";
Proteomics 2:591-602(2002).
[5]
CATALYTIC ACTIVITY, EXPRESSION, DISRUPTION PHENOTYPE, AND GENE NAME.
STRAIN=168;
PubMed=16233686; DOI=10.1263/jbb.98.174;
Yamaguchi H., Furuhata K., Fukushima T., Yamamoto H., Sekiguchi J.;
"Characterization of a new Bacillus subtilis peptidoglycan hydrolase
gene, yvcE (named cwlO), and the enzymatic properties of its encoded
protein.";
J. Biosci. Bioeng. 98:174-181(2004).
[6]
INDUCTION BY YYCFG.
PubMed=17581128; DOI=10.1111/j.1365-2958.2007.05782.x;
Bisicchia P., Noone D., Lioliou E., Howell A., Quigley S., Jensen T.,
Jarmer H., Devine K.M.;
"The essential YycFG two-component system controls cell wall
metabolism in Bacillus subtilis.";
Mol. Microbiol. 65:180-200(2007).
-!- FUNCTION: The C-terminal part of CwlO shows a cell wall hydrolytic
DL-endopeptidase activity.
-!- ACTIVITY REGULATION: Detected in exponentially growing cells, the
50 and 30 kDa processing products disappear upon entry into
stationary phase with the concomitant appearance of a 20 kDa
products. The 50 kDa form persists in the absence of extracellular
proteases (PubMed:11987133). {ECO:0000269|PubMed:11987133}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11987133}.
Secreted, cell wall {ECO:0000269|PubMed:11987133}.
-!- DEVELOPMENTAL STAGE: Expressed during the early stage of the
vegetative growth phase (PubMed:16233686). Not detected in
stationary phase (PubMed:11987133). {ECO:0000269|PubMed:11987133,
ECO:0000269|PubMed:16233686}.
-!- INDUCTION: Positively regulated by the two-component system YycFG.
{ECO:0000269|PubMed:17581128}.
-!- PTM: Identified in the extracellular proteome as a number of
processing products of about 50 and 30 kDa.
-!- DISRUPTION PHENOTYPE: Disruption of the cwlO gene affects neither
the vegetative cell growth rate, cell morphology, motility,
sporulation frequency nor the germination frequency.
{ECO:0000269|PubMed:16233686}.
-!- MISCELLANEOUS: The N-terminal part of CwlO was shown to have no
cell wall-binding activity.
-!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z94043; CAB08053.1; -; Genomic_DNA.
EMBL; AL009126; CAB15485.1; -; Genomic_DNA.
EMBL; M22901; AAA22817.1; ALT_FRAME; Genomic_DNA.
PIR; F70031; F70031.
RefSeq; NP_391360.1; NC_000964.3.
RefSeq; WP_009968231.1; NZ_JNCM01000033.1.
ProteinModelPortal; P40767; -.
SMR; P40767; -.
STRING; 224308.Bsubs1_010100018846; -.
MEROPS; C40.010; -.
PaxDb; P40767; -.
PRIDE; P40767; -.
DNASU; 936533; -.
EnsemblBacteria; CAB15485; CAB15485; BSU34800.
GeneID; 936533; -.
KEGG; bsu:BSU34800; -.
PATRIC; fig|224308.179.peg.3768; -.
eggNOG; COG0791; LUCA.
eggNOG; COG3883; LUCA.
HOGENOM; HOG000009133; -.
InParanoid; P40767; -.
KO; K21471; -.
OMA; MIPSANV; -.
PhylomeDB; P40767; -.
BioCyc; BSUB:BSU34800-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
InterPro; IPR000064; NLP_P60_dom.
InterPro; IPR038765; Papain_like_cys_pep_sf.
Pfam; PF00877; NLPC_P60; 1.
SUPFAM; SSF54001; SSF54001; 1.
1: Evidence at protein level;
Cell wall; Cell wall biogenesis/degradation; Complete proteome;
Hydrolase; Reference proteome; Secreted; Signal.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 473 Peptidoglycan DL-endopeptidase CwlO.
/FTId=PRO_0000213727.
COMPBIAS 291 352 Ser-rich.
ACT_SITE 377 377 Nucleophile. {ECO:0000250}.
ACT_SITE 431 431 Proton acceptor. {ECO:0000250}.
SEQUENCE 473 AA; 51033 MW; AF544B030E683038 CRC64;
MRKSLITLGL ASVIGTSSFL IPFTSKTASA ETLDEKKQKI ESKQSEVASS IEAKEKELTE
LQENQSKIEK ELKDINDKAL DTSNKIEDKK EENDKTKEEI KKLKKEIKET EARIEKRNEI
LKKRVRSLQE SGGSQGYIDV LLGSTSFGDF ISRATAVSSI VDADKDLIKQ QEQDKAKLED
SEADLNDKLK EVQAALAKLE TMQKDLDKQL NEKDKLFDEA KASQKKTAKA ISELKSEASE
LANQKANTEA EQARIKKEQE AAAALIKKQE EAQKASDETQ TDDSQTATTE SSKASSSDDS
SDNSSDNSSN GSSNSSSNGS SSKKSSGSNS NSGGTVISNS GGIEGAISVG SSIVGQSPYK
FGGGRTQSDI NNRIFDCSSF VRWAYASAGV NLGPVGGTTT DTLVGRGQAV SASEMKRGDL
VFFDTYKTNG HVGIYLGNGT FLNDNTSHGV SVDSMSNPYW KAAFKGVVRR VVQ


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