ID   B6EH15_ALISL            Unreviewed;       846 AA.
AC   B6EH15;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   Name=chiA {ECO:0000313|EMBL:CAQ78442.1};
GN   OrderedLocusNames=VSAL_I0757 {ECO:0000313|EMBL:CAQ78442.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ78442.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ78442.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ78442.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   EMBL; FM178379; CAQ78442.1; -; Genomic_DNA.
DR   RefSeq; WP_012549560.1; NC_011312.1.
DR   AlphaFoldDB; B6EH15; -.
DR   CAZy; CBM5; Carbohydrate-Binding Module Family 5.
DR   CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR   CAZy; GH18; Glycoside Hydrolase Family 18.
DR   KEGG; vsa:VSAL_I0757; -.
DR   eggNOG; COG3469; Bacteria.
DR   eggNOG; COG3979; Bacteria.
DR   HOGENOM; CLU_342135_0_0_6; -.
DR   Proteomes; UP000001730; Chromosome 1.
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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12215; ChiC_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   Gene3D; 2.60.40.10; Immunoglobulins; 4.
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   InterPro; IPR013783; Ig-like_fold.
DR   PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR   PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR   Pfam; PF17957; Big_7; 4.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 2.
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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..846
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002844354"
FT   DOMAIN          523..846
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   846 AA;  89752 MW;  1B7B7099FEAE7053 CRC64;
     MKRIFINSAI ASALFISYGA NAFDCSSLPL WQNSEPYSGG AEIQQNQIAY QAQWWSQGNS
     PETHSGEWQK WKRLGQCDNS GGNTAPTLSI ISPLNNAAIA EGSAITLQAN AVDSDGEITR
     VEFLADSQSI TIITAPPYNT DWVALKNTTS ISVIATDNEG SSTTESVSIR VQSTGDLIPP
     SIQLLSPTGN EVLSVGDDLL MSADAIDNDG QIAYVEFYVD SELVFTDSSA PFEHLWTATK
     GTHRFKAKAI DNDEQSSISQ ESILTITEPS SGGCAGLPQY KSGTAYTQGD EIQNINQKYR
     CDVGGWCSSS SDWAYAPGTG SSWQDAWTGL GVCSTPPEVA ITSPSDNSVI LAGSSIIINA
     TASDSDGSIV GVEFFANDMT LGADTQAPYS MTWTAALIGN NTLKAVATDN EGNNSDNSIL
     VTVSDQNVVT SLTSPASGSS LALGKVTQLS ATATSLTSSI TQVDFLINGA IVGSDTTTPY
     NTNWTPSAIG SYSISTEATD AQGNKALSIA SSIAVLEQSQ ATHKLIGYWH NFVNGSGCPI
     RLSEMPDEWD VIDIAFADND RNSNGTVHFN LYSGDIHSSC LALDPNQFKQ DMAALQAKGK
     IFVLSLGGAE GTITLNTEQD EANFVSSLTA LIDEWGFDGL DIDLESGSNL LHGTQIQARL
     PTALKQIEMN MGGDMYLTMA PEHPYVQGGM VAYSGIWGAY IPVIDQVRDT LDLLHVQLYN
     NGGLANPYMP GAAPEGSVDM MVASVKMLVE GFELADGSFF APLRDDQVAI GLPSGPSSAN
     SGQAPTQNII DALDCVTYGS ACSTVVPNKL YPNFGGVMTW SINWDKHDGF NFSQPIGEKL
     TLMNAQ
//