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}.
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; 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
//