LYTE_BACSU
ID LYTE_BACSU Reviewed; 334 AA.
AC P54421; O07574;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Probable peptidoglycan endopeptidase LytE;
DE EC=3.4.-.-;
DE AltName: Full=Cell wall-associated polypeptide CWBP33;
DE AltName: Full=Gamma-D-glutamate-meso-diaminopimelate muropeptidase LytE;
DE AltName: Full=Minor autolysin LytE;
DE AltName: Full=Phosphatase-associated protein PapQ;
DE AltName: Full=Vegetative cell wall hydrolase LytE;
DE Flags: Precursor;
GN Name=lytE; Synonyms=cwlF, papQ; OrderedLocusNames=BSU09420;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 26-36.
RC STRAIN=168;
RX PubMed=9457885; DOI=10.1128/jb.180.3.749-752.1998;
RA Margot P., Wahlen M., Gholamhuseinian A., Piggot P., Karamata D.;
RT "The lytE gene of Bacillus subtilis 168 encodes a cell wall hydrolase.";
RL J. Bacteriol. 180:749-752(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9579061; DOI=10.1099/00221287-144-4-859;
RA Noback M.A., Holsappel S., Kiewiet R., Terpstra P., Wambutt R., Wedler H.,
RA Venema G., Bron S.;
RT "The 172 kb prkA-addAB region from 83 degrees to 97 degrees of the Bacillus
RT subtilis chromosome contains several dysfunctional genes, the glyB marker,
RT many genes encoding transporter proteins, and the ubiquitous hit gene.";
RL Microbiology 144:859-875(1998).
RN [3]
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 [4]
RP SEQUENCE REVISION.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 311-334.
RC STRAIN=168 / SMY;
RX PubMed=8045898; DOI=10.1128/jb.176.15.4669-4679.1994;
RA Jin S., Sonenshein A.L.;
RT "Identification of two distinct Bacillus subtilis citrate synthase genes.";
RL J. Bacteriol. 176:4669-4679(1994).
RN [6]
RP PROTEIN SEQUENCE OF 26-45, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=9573210; DOI=10.1128/jb.180.9.2549-2555.1998;
RA Ishikawa S., Hara Y., Ohnishi R., Sekiguchi J.;
RT "Regulation of a new cell wall hydrolase gene, cwlF, which affects cell
RT separation in Bacillus subtilis.";
RL J. Bacteriol. 180:2549-2555(1998).
RN [7]
RP FUNCTION.
RC STRAIN=168;
RX PubMed=10322020; DOI=10.1128/jb.181.10.3178-3184.1999;
RA Ohnishi R., Ishikawa S., Sekiguchi J.;
RT "Peptidoglycan hydrolase LytF plays a role in cell separation with CwlF
RT during vegetative growth of Bacillus subtilis.";
RL J. Bacteriol. 181:3178-3184(1999).
RN [8]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RC STRAIN=168;
RX PubMed=14594841; DOI=10.1128/jb.185.22.6666-6677.2003;
RA Yamamoto H., Kurosawa S., Sekiguchi J.;
RT "Localization of the vegetative cell wall hydrolases LytC, LytE, and LytF
RT on the Bacillus subtilis cell surface and stability of these enzymes to
RT cell wall-bound or extracellular proteases.";
RL J. Bacteriol. 185:6666-6677(2003).
RN [9]
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: Cell wall hydrolase that cleaves gamma-D-glutamate-meso-
CC diaminopimelate bonds in peptidoglycan (By similarity). Seems to play a
CC role in cell separation during vegetative growth. {ECO:0000250,
CC ECO:0000269|PubMed:10322020, ECO:0000269|PubMed:14594841}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000269|PubMed:14594841}. Note=LytE is localized at cell
CC separation sites and cell poles of vegetative cells.
CC -!- INDUCTION: Expressed during the exponential growth phase, under the
CC control of SigA (major) and SigH (minor). Is also positively regulated
CC by the two-component system YycFG. {ECO:0000269|PubMed:17581128,
CC ECO:0000269|PubMed:9573210}.
CC -!- DOMAIN: The N-terminal domain contains LysM domains that are thought to
CC be involved in peptidoglycan binding, while the C-terminal domain is
CC endowed with the catalytic activity. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are about twice as long
CC as those of the wild-type strain. {ECO:0000269|PubMed:9573210}.
CC -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC ProRule:PRU01284, ECO:0000305}.
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DR EMBL; U38819; AAC25975.1; -; Genomic_DNA.
DR EMBL; Y14082; CAA74487.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12781.2; -; Genomic_DNA.
DR EMBL; U05256; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G69654; G69654.
DR RefSeq; NP_388823.2; NC_000964.3.
DR RefSeq; WP_003244816.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P54421; -.
DR SMR; P54421; -.
DR STRING; 224308.BSU09420; -.
DR CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR MEROPS; C40.003; -.
DR PaxDb; P54421; -.
DR PRIDE; P54421; -.
DR EnsemblBacteria; CAB12781; CAB12781; BSU_09420.
DR GeneID; 939269; -.
DR KEGG; bsu:BSU09420; -.
DR PATRIC; fig|224308.179.peg.1015; -.
DR eggNOG; COG0791; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR InParanoid; P54421; -.
DR OMA; YWSSMKS; -.
DR PhylomeDB; P54421; -.
DR BioCyc; BSUB:BSU09420-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; 3.
DR Gene3D; 3.10.350.10; -; 3.
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; 3.
DR Pfam; PF00877; NLPC_P60; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54106; SSF54106; 3.
DR PROSITE; PS51782; LYSM; 3.
DR PROSITE; PS51935; NLPC_P60; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Hydrolase; Protease; Reference proteome; Repeat; Secreted; Signal;
KW Thiol protease.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:9457885,
FT ECO:0000269|PubMed:9573210"
FT CHAIN 26..334
FT /note="Probable peptidoglycan endopeptidase LytE"
FT /id="PRO_0000019752"
FT DOMAIN 26..69
FT /note="LysM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 86..129
FT /note="LysM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 149..192
FT /note="LysM 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT DOMAIN 217..334
FT /note="NlpC/P60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT REGION 70..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 131..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 247
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 296
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT ACT_SITE 308
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT CONFLICT 16..46
FT /note="STLFAGAASAQSIKVKKGDTLWDLSRKYDTT -> ALFAHTSIRELKEHIVR
FT VLIRMRAMYKISEKRQYGLKKDK (in Ref. 2; CAA74487)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..103
FT /note="LWKISKKY -> FENFKKI (in Ref. 2; CAA74487)"
FT /evidence="ECO:0000305"
FT CONFLICT 137..144
FT /note="SSSSSKVS -> TPAHQKCA (in Ref. 2; CAA74487)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..158
FT /note="SGDS -> RETG (in Ref. 2; CAA74487)"
FT /evidence="ECO:0000305"
FT CONFLICT 164
FT /note="S -> R (in Ref. 2; CAA74487)"
FT /evidence="ECO:0000305"
FT CONFLICT 175..178
FT /note="SLNG -> RLKRA (in Ref. 2; CAA74487)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 35455 MW; D809C7DD4BAC475D CRC64;
MKKQIITATT AVVLGSTLFA GAASAQSIKV KKGDTLWDLS RKYDTTISKI KSENHLRSDI
IYVGQTLSIN GKSTSSKSSS SSSSSSTYKV KSGDSLWKIS KKYGMTINEL KKLNGLKSDL
LRVGQVLKLK GSTSSSSSSS SKVSSSSTST YKVKSGDSLS KIASKYGTTV SKLKSLNGLK
SDVIYVNQVL KVKGTSTSSS KPASSSSSSS SKTSSTSLNV SKLVSDAKAL VGTPYKWGGT
TTSGFDCSGF IWYVLNKQTS VGRTSTAGYW SSMKSIASPS VGDFVFFTTY KSGPSHMGIY
IGNNSFIHAG SDGVQISSLN NSYWKPRYLG AKRF
