ID A0A242K175_9ENTE Unreviewed; 578 AA.
AC A0A242K175;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Chitinase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A5844_001543 {ECO:0000313|EMBL:OTP11408.1};
OS Enterococcus sp. 10A9_DIV0425.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1987383 {ECO:0000313|EMBL:OTP11408.1, ECO:0000313|Proteomes:UP000194933};
RN [1] {ECO:0000313|EMBL:OTP11408.1, ECO:0000313|Proteomes:UP000194933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10A9_DIV0425 {ECO:0000313|EMBL:OTP11408.1,
RC ECO:0000313|Proteomes:UP000194933};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 10A9_DIV0425.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OTP11408.1}.
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DR EMBL; NGMO01000002; OTP11408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A242K175; -.
DR STRING; 1987383.A5844_001543; -.
DR Proteomes; UP000194933; Unassembled WGS sequence.
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; cd12214; ChiA1_BD; 1.
DR CDD; cd00063; FN3; 2.
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; 2.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
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; PTHR34823:SF1; CHITIN-BINDING TYPE-4 DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR34823; GLCNAC-BINDING PROTEIN A; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000194933};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..578
FT /note="Chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012196278"
FT DOMAIN 39..342
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 348..435
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 443..527
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT REGION 338..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 578 AA; 63258 MW; 3845DDE2EBCABB86 CRC64;
MNRKTLLFSV GLLGCLIGGG TNVFAADAAD TMPDISTKQI SVGYYHNWAS EYGAGYKGGR
PADIDLAKVN PFYNVISVAF MKGEGIPTFK PYNMSDQEFR AKVASLNAEG RAVLISLGGA
DSHIELHKGD EQSFANEIIR LVEVYGFDGL DIDLEQTAVA AGDNTTVIPE ALKIVRDHYQ
KEQKHFIISM APEFPYLRTQ GKYVPYITAL EEQYDFIAPQ LYNQAGDGIS VGSEWIAQNN
DSKKFEFLYG ISKAFNEGNN GFIKIPANRL ALGIPANEDA AANGFVQDPS KVYQVFEQMK
KDQTPLKGLM TWSIDWDEGR NSAGVMYNSG FAKSYQDLFG TPTPDTQKPS QPTNLRGTAT
SSSVSLSWQA STDNVSVASY NIYENDQLVG TSHTTNFTHS GLLADTVYTY KVEAVDTSGN
KSTLSDAFTI KTNELTQLPA PSVPDNLAVK GVTKSTVSLE WKANDQAEEI THYEVYRDGV
KVAESVAPIF EDKNLTVATT YSYQIKAVNA IGTSELTQKV MATTSNEQTE GEEWTIGKAY
VTGDIVTYNG KTYRCLQAHT AIATWAPDLV TSLWQLIG
//