ID   A0A0S2K7Q2_9GAMM        Unreviewed;      1052 AA.
AC   A0A0S2K7Q2;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   SubName: Full=Chitinase A {ECO:0000313|EMBL:ALO44305.1};
GN   ORFNames=PP2015_3836 {ECO:0000313|EMBL:ALO44305.1};
OS   Pseudoalteromonas phenolica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=161398 {ECO:0000313|EMBL:ALO44305.1, ECO:0000313|Proteomes:UP000061457};
RN   [1] {ECO:0000313|EMBL:ALO44305.1, ECO:0000313|Proteomes:UP000061457}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 12086 {ECO:0000313|EMBL:ALO44305.1,
RC   ECO:0000313|Proteomes:UP000061457};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC       class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR   EMBL; CP013188; ALO44305.1; -; Genomic_DNA.
DR   RefSeq; WP_058032173.1; NZ_CP013188.1.
DR   AlphaFoldDB; A0A0S2K7Q2; -.
DR   STRING; 161398.PP2015_3836; -.
DR   KEGG; pphe:PP2015_3836; -.
DR   PATRIC; fig|161398.10.peg.3921; -.
DR   OrthoDB; 9775889at2; -.
DR   Proteomes; UP000061457; Chromosome II.
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   CDD; cd06548; GH18_chitinase; 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; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR   InterPro; IPR032798; CBM_5_12_2.
DR   InterPro; IPR003610; CBM_fam5/12.
DR   InterPro; IPR036573; CBM_sf_5/12.
DR   InterPro; IPR009470; Chi_C.
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; IPR035986; PKD_dom_sf.
DR   PANTHER; PTHR11177; CHITINASE; 1.
DR   PANTHER; PTHR11177:SF308; CHITINASE A; 1.
DR   Pfam; PF17957; Big_7; 1.
DR   Pfam; PF14600; CBM_5_12_2; 1.
DR   Pfam; PF06483; ChiC; 1.
DR   Pfam; PF00704; Glyco_hydro_18; 1.
DR   SMART; SM00495; ChtBD3; 2.
DR   SMART; SM00636; Glyco_18; 1.
DR   SMART; SM00089; PKD; 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; PS01095; GH18_1; 1.
DR   PROSITE; PS51910; GH18_2; 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:UP000061457};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..1052
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006601355"
FT   DOMAIN          320..797
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
SQ   SEQUENCE   1052 AA;  114768 MW;  CCF709E20410ECB5 CRC64;
     MKDLNLMRKG FKPSALVLAI LSAPAFASVD CTNIPQWEAG KAYSEGMQAQ QDKVAYKSNW
     WNKAEPKLRS GDWQEWTKLG NCQTDVPVNE APKVTLLSPA NGNLLNENDS VAILAEASDT
     DGQVKQVEVY LDGQLLTTLN TAPFEFNWTA VVGEHVFYAI AQDDDGARTE SARHSVTVQK
     KSNENRAPVV SLAATLPSEL EVGSQVTFNL SVSDADGHAV SQTLTVNNEV VVNSTKGTEQ
     YVWTPTVAGT YTFTLTAKDE LGLAATPIER VYIVKEKGDP ITGHENCRPA GLYQAQGVQP
     AYCDIYDTEG REKMGADHPR RVIGYFTSWR NGANGQPSYL VKDIPWDKIT HINYAFAHVN
     AANELSIGDP NAAGNAATNM TWPGVEGAEM DPSLPYKGHF NLLNKYKKLH PDVKTMISVG
     GWAETGGFFD SNGNRVNSGG FYTMTTNADG SVNHAGIDAF VASAVKFIRE YGFDGVDIDY
     EYPSSMKDSG HPDDFPISNA RRAGLNASYD VLMRKLREAL DAASAQDNTH YMLTIASPSS
     GYLLRGMETF QTAKYLDFVN IMSYDLHGAW NDHVGHNAAL YDTGKDSELA QWNVYGTKEF
     EGIGYLNTDW AATYFRGALP AGRINIGLPY YTRGFRDVQG GENGLWGRAA LPNQADCAPG
     TGVGEKNKCG NGAVGIDNLW HDTVDGIEVP AGSNPLWHVK NLQNGITPSY LGVYGLDPVN
     NPEDKMVGTY TRHYDSVAIA PWLFNAEKKV FLSIEDEESM KTKLDYVVNK ELGGVMFWEL
     AGDFDYDTQK GEYFMGSTMT RLAYDTFNQA STPYGAHLGD GAFVPAAKAV DIKFEAKNFP
     VGDDNYPIRP TFAFTNNSQI DLTGATISFN IPVSTSAIFK SDWNAQKKLG IKIDTNNSNA
     AGNNIGGFEN EFHRASITLT NEWGGAAESF KPGETVNAQV LYYIPITGPV NFTIEKDGAS
     YAFASEYPKL PIATKPDTGN PGNGDPGNGT CNGVDVTTIN TYPNWPRTDW AGNPSHANAG
     DYIIHNQVVF QANWWTSKEP VEGGDWKKVC AL
//