ID A0A1Q4ZIB0_9ACTN Unreviewed; 295 AA.
AC A0A1Q4ZIB0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:OKI46530.1};
GN ORFNames=A6A29_27200 {ECO:0000313|EMBL:OKI46530.1};
OS Streptomyces sp. TSRI0281.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI46530.1, ECO:0000313|Proteomes:UP000186952};
RN [1] {ECO:0000313|EMBL:OKI46530.1, ECO:0000313|Proteomes:UP000186952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI46530.1,
RC ECO:0000313|Proteomes:UP000186952};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI46530.1}.
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DR EMBL; LWLE01000003; OKI46530.1; -; Genomic_DNA.
DR RefSeq; WP_073719440.1; NZ_LWLE01000003.1.
DR AlphaFoldDB; A0A1Q4ZIB0; -.
DR STRING; 1718998.A6A29_27200; -.
DR OrthoDB; 3614862at2; -.
DR Proteomes; UP000186952; Unassembled WGS sequence.
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:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd00325; chitinase_GH19; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 1.
DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR016283; Glyco_hydro_19.
DR InterPro; IPR000726; Glyco_hydro_19_cat.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR PANTHER; PTHR22595:SF208; CHITINASE; 1.
DR PANTHER; PTHR22595; CHITINASE-RELATED; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00182; Glyco_hydro_19; 1.
DR PIRSF; PIRSF001060; Endochitinase; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001060-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000186952};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..295
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011959355"
FT DOMAIN 33..75
FT /note="Chitin-binding type-3"
FT /evidence="ECO:0000259|SMART:SM00495"
FT ACT_SITE 148
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001060-1"
FT DISULFID 167..175
FT /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
FT DISULFID 263..295
FT /evidence="ECO:0000256|PIRSR:PIRSR001060-2"
SQ SEQUENCE 295 AA; 31136 MW; 0A318389D3AE3B4E CRC64;
MIRRVMSLLA ALGAVVATIV VLPATTAAAA DCAPAWNSSS VYTGGGSASY NGHNWSAKWW
TQNETPGTSD VWADKGSCGG GTDPGEPNPS GFVVSESQFN QMFPNRNSFY TYSGLTAALS
AYPGFANTGS DTVKRQEAAA FLANVSHETG GLVYIVEQNQ SNYPHYCDAT QPYGCPAGQA
AYYGRGPIQL SWNFNYKAAG DALGIDLLGN PYLVEQNASV AWKTGLWYWN TQNGPGTMTP
HNAMVNGAGF GETIRSINGS LECNGGNPGQ VQSRINKYTA FTQILGTTTG SNLSC
//
