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Database: UniProt
Entry: A0A0L7TAB1_9GAMM
LinkDB: A0A0L7TAB1_9GAMM
Original site: A0A0L7TAB1_9GAMM 
ID   A0A0L7TAB1_9GAMM        Unreviewed;       596 AA.
AC   A0A0L7TAB1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Chitinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NG42_14585 {ECO:0000313|EMBL:KOC88879.1}, NG43_14120
GN   {ECO:0000313|EMBL:KOC92303.1};
OS   Erwinia iniecta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC92303.1, ECO:0000313|Proteomes:UP000036851};
RN   [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B120 {ECO:0000313|EMBL:KOC88879.1,
RC   ECO:0000313|Proteomes:UP000037088}, and B149
RC   {ECO:0000313|EMBL:KOC92303.1, ECO:0000313|Proteomes:UP000036851};
RX   PubMed=26198254;
RA   Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA   Tisserat N.A., Leach J.E.;
RT   "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT   noxia).";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KOC92303.1}.
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DR   EMBL; JRXE01000020; KOC88879.1; -; Genomic_DNA.
DR   EMBL; JRXF01000021; KOC92303.1; -; Genomic_DNA.
DR   RefSeq; WP_052900212.1; NZ_JRXF01000021.1.
DR   AlphaFoldDB; A0A0L7TAB1; -.
DR   STRING; 1560201.NG42_14585; -.
DR   PATRIC; fig|1560201.3.peg.3099; -.
DR   OrthoDB; 315328at2; -.
DR   Proteomes; UP000036851; Unassembled WGS sequence.
DR   Proteomes; UP000037088; 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; 1.
DR   CDD; cd02871; GH18_chitinase_D-like; 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; 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; 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; SSF49265; Fibronectin type III; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037088};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..596
FT                   /note="Chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008219477"
FT   DOMAIN          43..333
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   DOMAIN          449..534
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000259|PROSITE:PS50853"
FT   REGION          341..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..463
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   596 AA;  64184 MW;  158398854A9D062D CRC64;
     MRSLFRKNMI TASLLMAGLL SCSASFAAAN DAASAFPDIS GKKVLVGFWH NWASKSDGYQ
     QGTAADVELT SIPEEYNVIT VAFMEGSGIP TFKPHNMTDA QFRQAVATLN SQGRAVLVSL
     GGAEAHIELK AGDAQKFADE IIRLVEVYGF DGLDIDLEGN AIKAGANQTE IPAALKIVKN
     KYPRFIISMA PEFPYLRNNG AYAGLINSLE GYYDFISPQY YNQGGDGVGE GSQWYGQDRD
     DIKADFLYYL TDSLVHGTRG FIKIPADKFV IGLPSNPDAA ATGYVRNEGD LRTAYERLIS
     QGTPIKGLMT WSINWDTGHS SAGNAYGYEF AHRYGKLIHE DFTGDPDTQA PTQPGKPALT
     ASSGQVAMTW APSSDNVGVA QYQIWRNGEE IGQSTVPQYN DNQVSNGNTY EYVIIAVDKA
     GNLSLPGEAA SVTLEENDTP SDDIEQPTVP QDLNGEATGP NSVNLSWEAS SDNVAVRHYN
     IYRNGALLTK ETQTSFTDSG LAAGTTYHYQ VAAVDTSDNM SDKSDMISVT TAAGENPQPG
     YPAYVAGTAY KAGDKVSSAG GVYECKPWPY TGWCAGAEWA YAPGTGSNWA DAWDKK
//
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