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Database: UniProt
Entry: E3BL82_9VIBR
LinkDB: E3BL82_9VIBR
Original site: E3BL82_9VIBR 
ID   E3BL82_9VIBR            Unreviewed;       922 AA.
AC   E3BL82;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Exochitinase {ECO:0000313|EMBL:EFP96178.1};
GN   ORFNames=VIBC2010_03702 {ECO:0000313|EMBL:EFP96178.1};
OS   Vibrio caribbeanicus ATCC BAA-2122.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP96178.1, ECO:0000313|Proteomes:UP000002943};
RN   [1] {ECO:0000313|EMBL:EFP96178.1, ECO:0000313|Proteomes:UP000002943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP96178.1,
RC   ECO:0000313|Proteomes:UP000002943};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
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:EFP96178.1}.
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DR   EMBL; AEIU01000076; EFP96178.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3BL82; -.
DR   STRING; 796620.VIBC2010_03702; -.
DR   eggNOG; COG3325; Bacteria.
DR   eggNOG; COG3979; Bacteria.
DR   OrthoDB; 9775889at2; -.
DR   Proteomes; UP000002943; 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; cd12204; CBD_like; 1.
DR   CDD; cd12215; ChiC_BD; 1.
DR   Gene3D; 3.10.50.10; -; 1.
DR   Gene3D; 2.10.10.20; Carbohydrate-binding module superfamily 5/12; 2.
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; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR035986; PKD_dom_sf.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 2.
DR   SMART; SM00636; Glyco_18; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51055; Carbohydrate binding domain; 2.
DR   SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS51910; GH18_2; 1.
PE   4: Predicted;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002943};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           35..922
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003167186"
FT   DOMAIN          67..481
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   922 AA;  101735 MW;  87255E2019714540 CRC64;
     MKQTNMRLNK VVRAMIVTGC IAGAMASTIT SANADEHPWV TGHGLTKTKI DSSKERYNTY
     KSDESLPPVS AYLSNWAHYQ QGYKPSIEAL SKYDTVILSF FGLCGTEIGD PAIPNAVQKL
     KEHCGKFNAK KFEIMTTDFW ADLQVGFPSA GISSGSKQWL EPNPSGMLGV MKKLADETDT
     KVAVSIFGWS LSNIASDAVK PENRKVFIAS LIRFLEAYPF VSQLDIDWEY PGIQGASENV
     FDPDNDARNY AEFITELRSA LNNAHREDVK IGIASGAPQD KIDAAELQNL ITAGVDTIHL
     MTYDFFGESW AEGLAHHTNL MSNASRDWSS DASIDYMINE LHIDPKRIQI GYANYSRNAI
     NANITSKSPL EGSFTKGENV MGTFEGASSQ INDIFTNYLK PHENNGLIPQ NGYHLFTDAE
     ANADYLYNKD NQVFVSFDTP RTVYAKAQYA RKHNLGGIFN WMGDPDEGLM LNAAREGLGY
     TRENTVIDMD KIINTCGENI ISPDECHDLT HLIDSDPGHA VHAEDVTTEY QPGRHYELLA
     TVDDNTEIKN VEWSLEAVSG VDAKDVVIAA NQGLSSSFEI KVADVVENIN ASFKVTVTFA
     DNKTSSATMK YKLKVDESIP VITDIVNPDE YIYGSGEAFN FNVIAEDSQS KQLNYQWQVT
     PSDTAISSGI NGSNLAIDIE KLANRPSYDV TASVTVTNHF GNTAESSATT KVKGDPSLNQ
     PPVASFDVSP ENAQQGDVIE MTSTSKDELV DELQYQWHVT FNGTDITVDQ KRGVTASFKA
     QDAGEYQVNL QVTDVFGVTG EYTQDVEVSE RLIPEQCDGI DPDADQYPAW VQGNTYLGDD
     VVSHNSLVYK AKYWTQTEPS ATAVEWTLMS NEVLPWNADA IYSTNDEVDH NGRHWQAQYY
     AEKGDEPGVA PMWKDVGEAV CP
//
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