ID Q7PC53_SACD2 Unreviewed; 1271 AA.
AC Q7PC53;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 133.
DE SubName: Full=Chitinase B {ECO:0000313|EMBL:DAA01334.1};
DE SubName: Full=Chitinase. Glycosyl Hydrolase family 18 {ECO:0000313|EMBL:ABD83125.1};
DE EC=3.2.1.14 {ECO:0000313|EMBL:ABD83125.1};
GN Name=chiB {ECO:0000313|EMBL:DAA01334.1};
GN Synonyms=chi18B {ECO:0000313|EMBL:ABD83125.1};
GN OrderedLocusNames=Sde_3870 {ECO:0000313|EMBL:ABD83125.1};
OS Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Saccharophagus.
OX NCBI_TaxID=203122 {ECO:0000313|EMBL:DAA01334.1};
RN [1] {ECO:0000313|EMBL:DAA01334.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2-40 {ECO:0000313|EMBL:DAA01334.1};
RX PubMed=12754233; DOI=10.1128/JB.185.11.3352-3360.2003;
RA Howard M.B., Ekborg N.A., Taylor L.E., Weiner R.M., Hutcheson S.W.;
RT "Genomic analysis and initial characterization of the chitinolytic system
RT of Microbulbifer degradans strain 2-40.";
RL J. Bacteriol. 185:3352-3360(2003).
RN [2] {ECO:0000313|EMBL:ABD83125.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=2-40;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Saunders E.H., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Richardson P., Weiner R.;
RT "Complete sequence of Saccharophagus degradans 2-40.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ABD83125.1, ECO:0000313|Proteomes:UP000001947}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2-40 {ECO:0000313|EMBL:ABD83125.1}, and 2-40 / ATCC 43961 / DSM
RC 17024 {ECO:0000313|Proteomes:UP000001947};
RX PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA Weiner R.M., Taylor L.E.II., Henrissat B., Hauser L., Land M.,
RA Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA Richardson P.M., Borovok I., Hutcheson S.;
RT "Complete genome sequence of the complex carbohydrate-degrading marine
RT bacterium, Saccharophagus degradans strain 2-40 T.";
RL PLoS Genet. 4:E1000087-E1000087(2008).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class II subfamily. {ECO:0000256|ARBA:ARBA00009121}.
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DR EMBL; CP000282; ABD83125.1; -; Genomic_DNA.
DR EMBL; BK001042; DAA01334.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7PC53; -.
DR SMR; Q7PC53; -.
DR STRING; 203122.Sde_3870; -.
DR CAZy; GH18; Glycoside Hydrolase Family 18.
DR KEGG; sde:Sde_3870; -.
DR eggNOG; COG3325; Bacteria.
DR HOGENOM; CLU_263909_0_0_6; -.
DR OrthoDB; 9775889at2; -.
DR BRENDA; 3.2.1.200; 7555.
DR Proteomes; UP000001947; Chromosome.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:InterPro.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR013540; ChitinaseA_N.
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; IPR014756; Ig_E-set.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF08329; ChitinaseA_N; 1.
DR Pfam; PF00704; Glyco_hydro_18; 2.
DR SMART; SM00636; Glyco_18; 2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 2.
DR SUPFAM; SSF54556; Chitinase insertion domain; 2.
DR SUPFAM; SSF81296; E set domains; 1.
DR PROSITE; PS01095; GH18_1; 2.
DR PROSITE; PS51910; GH18_2; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
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:UP000001947};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1271
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007710957"
FT DOMAIN 221..622
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 860..1269
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 19..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..188
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..638
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..678
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1271 AA; 135181 MW; 5FBAA6335D89AD4D CRC64;
MNLTKFAVAA LSVAVLSACG GGAGNSPSPG AGSNTNTESA SSSSSSSSSS STSSTSSSSS
SSSGSAEVNV DIDVDIDVEN GSSSSSSSGS SSSSTGGGDI TIIDEIESST SSSTSSSSSS
GATSSSSTSS SSSSSSSSSS SGATGSSSSS SGAGSTSSSS SSSSSSSSSS SSSSSSSSSS
SSSTGGGNAG VDAELGYSIG DVYAPSFDYT AVGGERKTDN YRVIGYYMPS LDGSFPPSAI
GEQQAQMLTH INYAFIGINS QLECDFIDVE KADAETQIIA ELQALKNWNA DLKILFSVGG
WAESNDAAET VSRYRDAFAP ANREHFVSSC VAFMQQHGFD GIDIDWEYPR AEDVDNFIAG
LAAMRNQLDA RGNGELVTIA GAGGAFFLSR YYSKLAAIVE QLDFINLMTY DLNGPWNGVT
KTNFHAHLYG NNQEPRFYNA LREADLGLTW EEIVERFPSP FELTVDAAIK QHLMMDIPRE
KIVMGVPFYG RAFFNTGSSN TGLYQTFNTP NGDPYVGDAS LLVGCEACEA RGEPRIATFN
DIQQLIEGNY GYTRHFDDQT KAPWLYHAEN NIFVTYDDAQ SLVYKTDYIK QQGLGGAMFW
HLGQDDSQFT LLATLHTELN GANAGSLQGG NSETDNTTDE TEGNNEDNTE QNPEENTDTE
ETETETETET ETETETETET SVEQPTAPTI AWMNTSYTGS SVTVTITWNM YWGTNGNQWQ
LWLDGEQVYS ANLTTNGQNA QTDSKIITIT GAGAHSVEVK LCNQQDINVS CASDSETITL
QGGSDGATSS SSSSTSSSSS SSSSSTGGST SSTSSSSSST SSSSSSSSSS SSSTSGGGET
DLSGVVYGEY NNTYKQTSDK IIVTYFVEWG IYGRDYHVNN IPASNLTHVL FGFIAMCGDN
PHASGGAQAA IASECADKQD FEVTLVDRFA NLEKTYPGDT WYDDTTGQDY NGNFGQLRKL
KAQHPHLKIL PSIGGWTMST PFYEMAKNEA NRAVFVESAV NFIKKYDFFD GVDIDWEYPV
YGGTAPELST AADRDAYTAL MRDLRAALDE LAEETGREYE ITSAVGAAPE KIAAVDYASA
TTYMDYIFLM SYDYMGAWAN TTGHHTPLYN NNEEREGFNT HASVQNLLTA GVPSSKLVVG
GAFYGRGWVG TQNTNAAKSD LFPLYGQASG AAKGTWEAGV QDYRDLYDNY IGTNGTGING
FSAHYDEIAE AAYLWNSSTG EFISYDSPRS IAAKADYVKQ YNLAGMLTWE IDGDNGQLLN
AINESFGNEK Q
//
