ID   CHI18_ENTFA             Reviewed;         348 AA.
AC   Q838S2;
DT   13-FEB-2019, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Chitinase {ECO:0000303|PubMed:22210154};
DE            EC=3.2.1.14 {ECO:0000269|PubMed:22210154};
DE   AltName: Full=EfChi18A {ECO:0000303|PubMed:22210154};
DE   Flags: Precursor;
GN   OrderedLocusNames=EF_0361 {ECO:0000312|EMBL:AAO80224.1};
OS   Enterococcus faecalis (strain ATCC 700802 / V583).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=226185;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700802 / V583;
RX   PubMed=12663927; DOI=10.1126/science.1080613;
RA   Paulsen I.T., Banerjei L., Myers G.S.A., Nelson K.E., Seshadri R.,
RA   Read T.D., Fouts D.E., Eisen J.A., Gill S.R., Heidelberg J.F., Tettelin H.,
RA   Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C.,
RA   DeBoy R.T., Durkin S.A., Kolonay J.F., Madupu R., Nelson W.C.,
RA   Vamathevan J.J., Tran B., Upton J., Hansen T., Shetty J., Khouri H.M.,
RA   Utterback T.R., Radune D., Ketchum K.A., Dougherty B.A., Fraser C.M.;
RT   "Role of mobile DNA in the evolution of vancomycin-resistant Enterococcus
RT   faecalis.";
RL   Science 299:2071-2074(2003).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND PATHWAY.
RX   PubMed=22210154; DOI=10.1016/j.jmb.2011.12.033;
RA   Vaaje-Kolstad G., Bohle L.A., Gaseidnes S., Dalhus B., Bjoras M.,
RA   Mathiesen G., Eijsink V.G.;
RT   "Characterization of the chitinolytic machinery of Enterococcus faecalis
RT   V583 and high-resolution structure of its oxidative CBM33 enzyme.";
RL   J. Mol. Biol. 416:239-254(2012).
CC   -!- FUNCTION: Involved in chitin degradation. Catalyzes the cleavage of
CC       glycosidic linkages in chitooligosaccharides and in alpha- and beta-
CC       chitin. Its activity on chitooligosaccharides increases considerably
CC       with degrees of polymerization (the initial rate of hydrolysis for
CC       GlcNAc5 is about 130-fold higher than that for GlcNAc3). Its activity
CC       is greatly stimulated in the presence of the lytic chitin monooxygenase
CC       EfCBM33A, which attacks the crystalline structure of chitin and makes
CC       the polymer more accessible to the chitinase; combining the two enzymes
CC       leads to rapid and complete depolymerization of crystalline chitin,
CC       especially with beta-chitin as a substrate. Is likely involved in a
CC       chitin degradation pathway that allows E.faecalis V583 to grow on
CC       chitin as a carbon source. {ECO:0000269|PubMed:22210154}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC         Evidence={ECO:0000269|PubMed:22210154};
CC   -!- PATHWAY: Glycan degradation; chitin degradation.
CC       {ECO:0000269|PubMed:22210154}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22210154}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016830; AAO80224.1; -; Genomic_DNA.
DR   RefSeq; NP_814153.1; NC_004668.1.
DR   RefSeq; WP_010773692.1; NZ_KE136524.1.
DR   AlphaFoldDB; Q838S2; -.
DR   SMR; Q838S2; -.
DR   STRING; 226185.EF_0361; -.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   EnsemblBacteria; AAO80224; AAO80224; EF_0361.
DR   KEGG; efa:EF0361; -.
DR   PATRIC; fig|226185.45.peg.2968; -.
DR   eggNOG; COG3469; Bacteria.
DR   HOGENOM; CLU_067535_0_0_9; -.
DR   OMA; NGVHPPF; -.
DR   UniPathway; UPA00349; -.
DR   Proteomes; UP000001415; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
DR   GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
DR   GO; GO:0006032; P:chitin catabolic process; IDA:UniProtKB.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR011583; Chitinase_II.
DR   InterPro; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Chitin degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..348
FT                   /note="Chitinase"
FT                   /id="PRO_5004300419"
FT   DOMAIN          42..348
FT                   /note="GH18"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
FT   ACT_SITE        161
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01258"
SQ   SEQUENCE   348 AA;  38339 MW;  2CB9F395A6BF6DD8 CRC64;
     MKLKKIIPAF PLLSTVAVGL WLTPTQASAD AADTMVDISG KKVLVGYWHN WASKGRDGYK
     QGTSASLNLS EVNQAYNVVP VSFMKSDGTT RIPTFKPYNQ TDTAFRQEVA QLNSQGRAVL
     LALGGADAHI QLVKGDEQAF ANEIIRQVET YGFDGLDIDL EQLAITAGDN QTVIPATLKI
     VKDHYRAQGK NFIITMAPEF PYLKPGAAYE TYITSLNGYY DYIAPQLYNQ GGDGVWVDEI
     MTWVAQSNDA LKYEFLYYMS DSLIHGTRGY LQIPNDKLVL GLPANRDAAG SGYVVEATPV
     AKTFDQLAKD GNPIRGLMTW SANWDVGQDV NGKSYNNEFA TRYSNLVK