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Database: UniProt
Entry: Q7NTW8_CHRVO
LinkDB: Q7NTW8_CHRVO
Original site: Q7NTW8_CHRVO 
ID   Q7NTW8_CHRVO            Unreviewed;       439 AA.
AC   Q7NTW8;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 127.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   OrderedLocusNames=CV_2935 {ECO:0000313|EMBL:AAQ60603.1};
OS   Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC
OS   12614 / NCIMB 9131 / NCTC 9757).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Chromobacterium.
OX   NCBI_TaxID=243365 {ECO:0000313|EMBL:AAQ60603.1, ECO:0000313|Proteomes:UP000001424};
RN   [1] {ECO:0000313|EMBL:AAQ60603.1, ECO:0000313|Proteomes:UP000001424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 /
RC   NCTC 9757 {ECO:0000313|Proteomes:UP000001424};
RX   PubMed=14500782; DOI=10.1073/pnas.1832124100;
RA   Vasconcelos A.T.R., de Almeida D.F., Almeida F.C., de Almeida L.G.P.,
RA   de Almeida R., Goncalves J.A.A., Andrade E.M., Antonio R.V., Araripe J.,
RA   de Araujo M.F.F., Filho S.A., Azevedo V., Batista A.J., Bataus L.A.M.,
RA   Batista J.S., Belo A., vander Berg C., Blamey J., Bogo M., Bonato S.,
RA   Bordignon J., Brito C.A., Brocchi M., Burity H.A., Camargo A.A.,
RA   Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B.,
RA   Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Pasa T.B.C., Duran N.,
RA   Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S.,
RA   Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A.,
RA   Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B.,
RA   Grattapaglia D., Grisard E.C., Guimaraes C.T., Hanna E.S., Hungria M.,
RA   Jardim S.N., Laurino J., Leoi L.C.T., Fassarella L., Lima A.,
RA   Loureiro M.F., Lyra M.C.P., Macedo M., Madeira H.M.F., Manfio G.P.,
RA   Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B.,
RA   Meissner R.D.V., Menck C.F.M., Moreira M.A.M., Nascimento F.F.,
RA   Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A.,
RA   Pedrosa F.O., Pena S.J.D., Perreira J.O., Perreira M., Pinto L.S.R.C.,
RA   Pinto L.S., Porto J.I.R., Potrich D.P., Neto C.E.R., Reis A.M.M.,
RA   Rigo L.U., Rondinelli E., dos Santos E.B.P., Santos F.R., Schneider M.P.C.,
RA   Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R.,
RA   Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M.,
RA   Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R.,
RA   Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.;
RT   "The complete genome sequence of Chromobacterium violaceum reveals
RT   remarkable and exploitable bacterial adaptability.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003).
RN   [2] {ECO:0007829|PDB:4TX8}
RP   X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS), AND DISULFIDE BONDS.
RA   Pereira H.M., Lobo M.D.P., Brandao-Neto J., Grangeiro T.B.;
RT   "Crystal Structure of a Family GH18 Chitinase from Chromobacterium
RT   violaceum.";
RL   Submitted (JUL-2014) to the PDB data bank.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; AE016825; AAQ60603.1; -; Genomic_DNA.
DR   PDB; 4TX8; X-ray; 2.17 A; A=1-439.
DR   PDBsum; 4TX8; -.
DR   AlphaFoldDB; Q7NTW8; -.
DR   SMR; Q7NTW8; -.
DR   STRING; 243365.CV_2935; -.
DR   CAZy; CBM12; Carbohydrate-Binding Module Family 12.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   KEGG; cvi:CV_2935; -.
DR   eggNOG; COG3469; Bacteria.
DR   eggNOG; COG3979; Bacteria.
DR   HOGENOM; CLU_019399_1_1_4; -.
DR   OrthoDB; 315328at2; -.
DR   Proteomes; UP000001424; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12214; ChiA1_BD; 1.
DR   CDD; cd02871; GH18_chitinase_D-like; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
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   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:4TX8}; Calcium {ECO:0007829|PDB:4TX8};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Metal-binding {ECO:0007829|PDB:4TX8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001424};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..439
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004289059"
FT   DOMAIN          107..420
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          72..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        80..101
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:4TX8"
FT   BINDING         220
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:4TX8"
FT   BINDING         255
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0007829|PDB:4TX8"
FT   BINDING         353
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:4TX8"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0007829|PDB:4TX8"
FT   DISULFID        26..77
FT                   /evidence="ECO:0007829|PDB:4TX8"
FT   DISULFID        372..379
FT                   /evidence="ECO:0007829|PDB:4TX8"
SQ   SEQUENCE   439 AA;  45719 MW;  197F8D9FC0AAE035 CRC64;
     MRRTTGRAIA MAMLLALGQH AWAAACPGWA EGTAYKVGDV VSYNNANYTA LVAHTAYVGA
     NWNPAASPTL WTPGGSCAGG DPTPPTPPNP PTPPSPPPGN TVPFAKHALV GYWHNFANPS
     GSAFPLSQVS ADWDVIVVAF ADDAGNGNVS FTLDPAAGSA AQFIQDIRAQ QAKGKKVVLS
     LGGQNGSVTL NNATQVQNFV NSLYGILTQY GFDGIDLDLE SGSGIVVGAP VVSNLVSAVK
     QLKAKIGPNF YLSMAPEHPY VQGGFVAYGG NWGAYLPIID GLRDDLSVIH VQYYNNGGLY
     TPYSTGVLAE GSADMLVGGS KMLIEGFPIA NGASGSFKGL RPDQVAFGVP SGRSSANSGF
     VTADTVAKAL TCLTTLQGCG SVKPAQAYPA FRGVMTWSIN WDRRDGYTFS RPVAASLRQQ
     PVAAQAGKKK AARATRTAW
//
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