CWLO_BACSU
ID CWLO_BACSU Reviewed; 473 AA.
AC P40767; O06969;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Peptidoglycan DL-endopeptidase CwlO;
DE EC=3.4.-.-;
DE AltName: Full=D-gamma-glutamyl-meso-diaminopimelyl DL-endopeptidase;
DE AltName: Full=PSPA2;
DE Flags: Precursor;
GN Name=cwlO; Synonyms=yvcE, yzkA; OrderedLocusNames=BSU34800;
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;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-71.
RX PubMed=3145906; DOI=10.1016/0378-1119(88)90207-7;
RA Smith H., de Jong A., Bron S., Venema G.;
RT "Characterization of signal-sequence-coding regions selected from the
RT Bacillus subtilis chromosome.";
RL Gene 70:351-361(1988).
RN [4]
RP ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=168;
RX PubMed=11987133;
RX DOI=10.1002/1615-9861(200205)2:5<591::aid-prot591>3.0.co;2-8;
RA Antelmann H., Yamamoto H., Sekiguchi J., Hecker M.;
RT "Stabilization of cell wall proteins in Bacillus subtilis: a proteomic
RT approach.";
RL Proteomics 2:591-602(2002).
RN [5]
RP CATALYTIC ACTIVITY, EXPRESSION, DISRUPTION PHENOTYPE, AND GENE NAME.
RC STRAIN=168;
RX PubMed=16233686; DOI=10.1263/jbb.98.174;
RA Yamaguchi H., Furuhata K., Fukushima T., Yamamoto H., Sekiguchi J.;
RT "Characterization of a new Bacillus subtilis peptidoglycan hydrolase gene,
RT yvcE (named cwlO), and the enzymatic properties of its encoded protein.";
RL J. Biosci. Bioeng. 98:174-181(2004).
RN [6]
RP INDUCTION BY YYCFG.
RX PubMed=17581128; DOI=10.1111/j.1365-2958.2007.05782.x;
RA Bisicchia P., Noone D., Lioliou E., Howell A., Quigley S., Jensen T.,
RA Jarmer H., Devine K.M.;
RT "The essential YycFG two-component system controls cell wall metabolism in
RT Bacillus subtilis.";
RL Mol. Microbiol. 65:180-200(2007).
CC -!- FUNCTION: The C-terminal part of CwlO shows a cell wall hydrolytic DL-
CC endopeptidase activity.
CC -!- ACTIVITY REGULATION: Detected in exponentially growing cells, the 50
CC and 30 kDa processing products disappear upon entry into stationary
CC phase with the concomitant appearance of a 20 kDa products. The 50 kDa
CC form persists in the absence of extracellular proteases
CC (PubMed:11987133). {ECO:0000269|PubMed:11987133}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11987133}. Secreted,
CC cell wall {ECO:0000269|PubMed:11987133}.
CC -!- DEVELOPMENTAL STAGE: Expressed during the early stage of the vegetative
CC growth phase (PubMed:16233686). Not detected in stationary phase
CC (PubMed:11987133). {ECO:0000269|PubMed:11987133,
CC ECO:0000269|PubMed:16233686}.
CC -!- INDUCTION: Positively regulated by the two-component system YycFG.
CC {ECO:0000269|PubMed:17581128}.
CC -!- PTM: Identified in the extracellular proteome as a number of processing
CC products of about 50 and 30 kDa.
CC -!- DISRUPTION PHENOTYPE: Disruption of the cwlO gene affects neither the
CC vegetative cell growth rate, cell morphology, motility, sporulation
CC frequency nor the germination frequency. {ECO:0000269|PubMed:16233686}.
CC -!- MISCELLANEOUS: The N-terminal part of CwlO was shown to have no cell
CC wall-binding activity.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; Z94043; CAB08053.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15485.1; -; Genomic_DNA.
DR EMBL; M22901; AAA22817.1; ALT_FRAME; Genomic_DNA.
DR PIR; F70031; F70031.
DR RefSeq; NP_391360.1; NC_000964.3.
DR RefSeq; WP_009968231.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P40767; -.
DR SMR; P40767; -.
DR STRING; 224308.BSU34800; -.
DR MEROPS; C40.010; -.
DR PaxDb; P40767; -.
DR PRIDE; P40767; -.
DR DNASU; 936533; -.
DR EnsemblBacteria; CAB15485; CAB15485; BSU_34800.
DR GeneID; 936533; -.
DR KEGG; bsu:BSU34800; -.
DR PATRIC; fig|224308.179.peg.3768; -.
DR eggNOG; COG0791; Bacteria.
DR eggNOG; COG3883; Bacteria.
DR InParanoid; P40767; -.
DR OMA; RRIGEQD; -.
DR PhylomeDB; P40767; -.
DR BioCyc; BSUB:BSU34800-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR000064; NLP_P60_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF00877; NLPC_P60; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Hydrolase; Protease;
KW Reference proteome; Secreted; Signal; Thiol protease.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..473
FT /note="Peptidoglycan DL-endopeptidase CwlO"
FT /id="PRO_0000213727"
FT DOMAIN 340..471
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT REGION 31..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..337
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 377
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 431
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 443
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
SQ 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
