ID E2Q445_STRCL Unreviewed; 620 AA.
AC E2Q445;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=SCLAV_3909 {ECO:0000313|EMBL:EFG08983.1};
OS Streptomyces clavuligerus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1901 {ECO:0000313|EMBL:EFG08983.1, ECO:0000313|Proteomes:UP000002357};
RN [1] {ECO:0000313|EMBL:EFG08983.1, ECO:0000313|Proteomes:UP000002357}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27064 / DSM 738 / JCM 4710 / NBRC 13307 / NCIMB 12785 /
RC NRRL 3585 / VKM Ac-602 {ECO:0000313|Proteomes:UP000002357};
RX PubMed=20624727; DOI=10.1093/gbe/evq013;
RA Medema M.H., Trefzer A., Kovalchuk A., van den Berg M., Mueller U.,
RA Heijne W., Wu L., Alam M.T., Ronning C.M., Nierman W.C., Bovenberg R.A.L.,
RA Breitling R., Takano E.;
RT "The sequence of a 1.8-mb bacterial linear plasmid reveals a rich
RT evolutionary reservoir of secondary metabolic pathways.";
RL Genome Biol. Evol. 2:212-224(2010).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; CM000913; EFG08983.1; -; Genomic_DNA.
DR AlphaFoldDB; E2Q445; -.
DR STRING; 1901.BB341_09185; -.
DR eggNOG; COG3469; Bacteria.
DR Proteomes; UP000002357; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd00063; FN3; 1.
DR CDD; cd02871; GH18_chitinase_D-like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR003305; CenC_carb-bd.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR008979; Galactose-bd-like_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; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF02018; CBM_4_9; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00060; FN3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000002357};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 65..87
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 239..320
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 331..620
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 620 AA; 64192 MW; B486BA2A64AECF1B CRC64;
MGRPGRNPMD DSRRPSRAGV LTSALVWTNL GGQRWPPFTP PCPSQSPQLP HWRQHVDRST
RSRRWLGGGL ALAVGAGLTV TGLTGVAQAA DINVAKNPGF ESGLSSWTCS GGSGSNVPSP
VRTGTSALRA APAGHDNARC SQSVAVKPNS TYQLSAWTQG GHAYLGASGT GTTDISTWSP
GSTGWQQLST SFRTGPSTTS VTVYTHGWYG TPAYFVDDVS VFGPDGGGGP DPEPVIPPTP
TGLATGQVTS SSVALNWGAA NGATGYNVYR DGTKVQSATG TSATVTGLTA NTSYQFQVTA
TNSAGESARS TAVTARTSSG PVIPNPVVPR HAVTGYWQNF NNGATVQKLR DVQNAYDIIA
VAFADATNTP GELTFNLSPA LGYSSVAEFK SDIAAKKAAG KSVIISVGGE IGNVTINSDA
SATAFANSAW ALMQEYGFNG IDIDLEHGIN STYLTKALRQ LSAKAGPNMV LTMAPQTIDM
QSTSTEYFKL ALNVKDILTV VNMQNYNSGA MLGCDGKVYS LGSVDFLTAL ACIQLENGLD
PSQVGLGVPA STRGAGSGYV SPATVTAALD CLTRATNCGS FKPPRTYPAL RGAMTWSTNW
DATAGNAWSN AVGPHVKALP
//
