(data stored in SCRATCH zone)

SWISSPROT: D3UYQ1_XENBS

ID   D3UYQ1_XENBS            Unreviewed;      1023 AA.
AC   D3UYQ1;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 51.
DE   RecName: Full=Lysozyme {ECO:0000256|RuleBase:RU003788};
DE            EC=3.2.1.17 {ECO:0000256|RuleBase:RU003788};
GN   OrderedLocusNames=XBJ1_0278 {ECO:0000313|EMBL:CBJ79429.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79429.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79429.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79429.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-linkages between N-
CC         acetylmuramic acid and N-acetyl-D-glucosamine residues in a
CC         peptidoglycan and between N-acetyl-D-glucosamine residues in
CC         chitodextrins.; EC=3.2.1.17;
CC         Evidence={ECO:0000256|RuleBase:RU003788};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 24 family.
CC       {ECO:0000256|RuleBase:RU003788}.
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DR   EMBL; FN667741; CBJ79429.1; -; Genomic_DNA.
DR   STRING; 406818.XBJ1_0278; -.
DR   CAZy; GH24; Glycoside Hydrolase Family 24.
DR   EnsemblBacteria; CBJ79429; CBJ79429; XBJ1_0278.
DR   KEGG; xbo:XBJ1_0278; -.
DR   eggNOG; ENOG4105CS6; Bacteria.
DR   eggNOG; COG3501; LUCA.
DR   eggNOG; COG3772; LUCA.
DR   HOGENOM; HOG000148858; -.
DR   KO; K11904; -.
DR   OMA; MFAYNIG; -.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0003796; F:lysozyme activity; IEA:UniProtKB-EC.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR   Gene3D; 2.40.50.230; -; 1.
DR   InterPro; IPR002196; Glyco_hydro_24.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR017847; T6SS_RhsGE_Vgr_subset.
DR   InterPro; IPR006533; T6SS_Vgr_RhsGE.
DR   InterPro; IPR037026; Vgr_OB-fold_dom_sf.
DR   Pfam; PF00959; Phage_lysozyme; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   TIGRFAMs; TIGR01646; vgr_GE; 1.
DR   TIGRFAMs; TIGR03361; VI_Rhs_Vgr; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UYQ1.
DR   SWISS-2DPAGE; D3UYQ1.
KW   Antimicrobial {ECO:0000256|RuleBase:RU003788};
KW   Bacteriolytic enzyme {ECO:0000256|RuleBase:RU003788};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Glycosidase {ECO:0000256|RuleBase:RU003788,
KW   ECO:0000313|EMBL:CBJ79429.1};
KW   Hydrolase {ECO:0000256|RuleBase:RU003788,
KW   ECO:0000313|EMBL:CBJ79429.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
SQ   SEQUENCE   1023 AA;  108163 MW;  12F79B0131CF8EB3 CRC64;
     MSMKKNMAKL KKGRALIQQG QQAAQLAKHV TGKLGGGLGG AAAGTAGLIP GGGFGGGIGG
     GSAGTGAAGL IPGGGFGGGL GGAGGGAGQG LAARAASGQS GAAKALQKAG QLLGGGGGMA
     PSGLQFTLTA GGLPPETFVV TDFALTEGFS RPFSLHVGLA SADPAIDFPA VLDRSATLTI
     LQEGVEQRSI TGIVARFEQG NTGLHQTTYQ MSLYPDLWRT TLRQNSRIFQ QLDIAAILTT
     LLKEHGIRDV VFSLRHPHPA REFCVQYQES DFAFLQRLTA EEGIFYFFEC GNGRNTLVFA
     DDAGSVPPGI VLAYQPGEGS TTGTPSVGSF TCSAQVRPAQ VQLKDYTFKN PAWPAEFSQQ
     MKEDTLQQMY YEHYDYPGRF KDEAHGQAFT RYRLEALRSD AVTGQASGQA IAVQPGKLFT
     LFNHPREDLN QPWQVVGASH TGSQPQARET ASSDSGTTLH SQFSFIRHNQ HWRPAPLPKP
     TIDGPQIAKV VGPAGEEIFC DQYGRIRLQF PWDRYGKSDD QSSCWIRVSQ PWAGQGWGML
     AIPRIGQEVV VDFLHGDPDQ PIVTGRTYHA SNIPPGALPG SKTQMAFRSK THKGEGYNEL
     LFEDAKGSER LALHAQKDMH TTVKDNQSLV VEAGDRTLTV QTGDEHKTVK QGNLTETICQ
     TRSTEANVIQ VKAKAGKAGL GTQLYQAEDN ITLQVGKGSI EMTPEHIRVA FGSSVILLNS
     SGVFVDGPAI GLNNGSAGAG LPPAAADGGD SASESGSLLP AAVMAAGLGP MGMAALGSMG
     LISSASAATP ASAPRPMPTP ADGAGRQAAP ADSQATPASA PRSMPVPVNG AGRQAVPAGS
     QVAAPSAPPV SATNLTTSTK KTMGQDGLDL LKGIESLRLK PYDDQTGKTV TKWTKGATIG
     YGKLIEKKDW DTYKDGITED EAEELFKKTL APFEKTVNDG ITKEINQNQF DALTMFAYNI
     GAKGFNDSSV LKLVNDENAK TDYDTLDDAW KAWNKSQGKV NQGVINRRAA ELKIYNEGVY
     ERW
//

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