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Database: UniProt
Entry: G2NQ72_STREK
LinkDB: G2NQ72_STREK
Original site: G2NQ72_STREK 
ID   G2NQ72_STREK            Unreviewed;       507 AA.
AC   G2NQ72;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=Chitinase {ECO:0000313|EMBL:AEN13553.1};
DE            EC=3.2.1.14 {ECO:0000313|EMBL:AEN13553.1};
DE   Flags: Precursor;
GN   ORFNames=SACTE_5764 {ECO:0000313|EMBL:AEN13553.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN13553.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN13553.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA   Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEN13553.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX   PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA   Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical properties and atomic resolution structure of a
RT   proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT   SirexAA-E.";
RL   PLoS ONE 9:e94166-E94166(2014).
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DR   EMBL; CP002993; AEN13553.1; -; Genomic_DNA.
DR   RefSeq; WP_014049503.1; NC_015953.1.
DR   AlphaFoldDB; G2NQ72; -.
DR   STRING; 862751.SACTE_5764; -.
DR   KEGG; ssx:SACTE_5764; -.
DR   PATRIC; fig|862751.12.peg.5978; -.
DR   eggNOG; COG3325; Bacteria.
DR   eggNOG; COG3979; Bacteria.
DR   HOGENOM; CLU_019399_3_0_11; -.
DR   OrthoDB; 99456at2; -.
DR   Proteomes; UP000001397; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd12215; ChiC_BD; 1.
DR   CDD; cd06543; GH18_PF-ChiA-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; IPR001223; Glyco_hydro18_cat.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR42976; BIFUNCTIONAL CHITINASE/LYSOZYME-RELATED; 1.
DR   PANTHER; PTHR42976:SF1; GH18 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02839; CBM_5_12; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000313|EMBL:AEN13553.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEN13553.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           34..507
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003433865"
FT   DOMAIN          40..347
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   507 AA;  52303 MW;  0F34E97F6CD767AB CRC64;
     MRRSRSVRAL VTAAVTTVAA AGMAVLGSGT AQAATPLPDH VFAPYFESWT GESPAAMAAE
     SGAKHLTMAF LQTTAKGSCT PYWNGDTGLP IAQASFGADI DTIQAGGGDV IPSFGGYTAD
     TTGTEIADSC TDVDQIAAAY QKVVTTYDVS RLDMDIEVDS LDDTAGIDRR NKAIKKLQDW
     ADANGRDLEI SYTLPTTTRG LASSGLAVLR NAVTNGARVD VVNLMTFDYY DNASHDMAAD
     TETAAQGLYD QLAKLYPGRT ATQLWSMVGV TEMPGVDDFG PAETFTLANA ARVYDWAVAK
     GINTLSFWAL QRDNGGCPGG PAADDCSGIQ QNTWDFTRVF APFTSGTTAP DDDFSVTATP
     ASGTVTAGGS ATTTVKTAVT KGAAQQVGLT VSGVPAGVTA SLSPSSVTAG GRSTLTLATT
     QAAVSGTYRI SVTGTSPSGS HATAYTLTVT GGTGSQCTAG PWAGGTVYTG GQQVSYKGHT
     WKAKWWTTGE EPGTTGEWGV WQDLGAC
//
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