ID A4BBI0_9GAMM Unreviewed; 545 AA.
AC A4BBI0;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Putative chitinase C {ECO:0000313|EMBL:EAR10315.1};
GN ORFNames=MED297_00800 {ECO:0000313|EMBL:EAR10315.1};
OS Reinekea blandensis MED297.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Reinekea.
OX NCBI_TaxID=314283 {ECO:0000313|EMBL:EAR10315.1, ECO:0000313|Proteomes:UP000005953};
RN [1] {ECO:0000313|EMBL:EAR10315.1, ECO:0000313|Proteomes:UP000005953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MED297 {ECO:0000313|EMBL:EAR10315.1,
RC ECO:0000313|Proteomes:UP000005953};
RA Pinhassi J., Pedros-Alio C., Ferriera S., Johnson J., Kravitz S.,
RA Halpern A., Remington K., Beeson K., Tran B., Rogers Y.-H., Friedman R.,
RA Venter J.C.;
RL Submitted (FEB-2006) 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:EAR10315.1}.
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DR EMBL; AAOE01000004; EAR10315.1; -; Genomic_DNA.
DR AlphaFoldDB; A4BBI0; -.
DR STRING; 314283.MED297_00800; -.
DR HOGENOM; CLU_002833_14_4_6; -.
DR Proteomes; UP000005953; 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:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd12215; ChiC_BD; 1.
DR CDD; cd06548; GH18_chitinase; 1.
DR CDD; cd00146; PKD; 1.
DR Gene3D; 3.10.50.10; -; 1.
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; 1.
DR InterPro; IPR003610; CBM_fam5/12.
DR InterPro; IPR036573; CBM_sf_5/12.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_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 InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF02839; CBM_5_12; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR Pfam; PF18911; PKD_4; 1.
DR SMART; SM00495; ChtBD3; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SMART; SM00089; PKD; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51055; Carbohydrate binding domain; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF49299; PKD domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
DR PROSITE; PS50093; PKD; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
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:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000005953};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..545
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002666576"
FT DOMAIN 88..169
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 180..545
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 59..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 545 AA; 58551 MW; 84F778EC501112DD CRC64;
MIGLRHILTG AAVALTMSSS LFAADCNGVA EWQPTTVYLG GDQATQNNQL YTAAWWTQNQ
SPETHSGPWQ EWKHQGECEG TNPPGNEPPT AIINGPFSAK VGDTIAMNAT ASSDADGFIE
SYSWTFGDGA SSNEMNPAHQ YNAEGTYDVT LEVTDDDGAK AVAKTTATIS NDTPPPTTDA
KVIGYFAEWG VYGRDYHVKD IATSGSADRL THILYAFGNV KNGKCTVGDS YAAYDKAYSA
ADSVDGVADT WDTGALRGNI GQFKRLKEMY PHLKIIWSFG GWTWSGGFGE AAQNPDAFAE
SCYQLINDPR WAGVFDGIDI DWEYPNECGL TCDNSGFDGY RNLMAALRAR FGTQLVTSAI
GAAEAKLRAA DYGGAAPYVD FYMLMTYDYF GAFNPQGPTA PHSPLYSYNG IPTDGFYSDK
GIQVLKSLGV PSDKILLGIG FYGRGWTGVT QSAPGGSASG AAQGEYEAGI NDYKILKQSC
PATGLIAGTA YAHCGNNWWS YDTPQTIQSK MDYVKQQGLD GAFFWELSGD TADGELIRAI
DNGLK
//
