ID   CBPD_PSEAB              Reviewed;         389 AA.
AC   Q02I11;
DT   07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Chitin-binding protein CbpD;
DE   Flags: Precursor;
GN   Name=cpbD; OrderedLocusNames=PA14_53250;
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, AND
RP   PHOSPHORYLATION AT TYR-37 AND SER-210.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=24965220; DOI=10.1002/pmic.201400190;
RA   Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT   "Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas
RT   aeruginosa PA14 strain.";
RL   Proteomics 14:2017-2030(2014).
CC   -!- FUNCTION: Binds but does not hydrolyze chitin.
CC       {ECO:0000250|UniProtKB:Q9I589}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24965220}.
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DR   EMBL; CP000438; ABJ10011.1; -; Genomic_DNA.
DR   RefSeq; WP_003140848.1; NZ_CP034244.1.
DR   AlphaFoldDB; Q02I11; -.
DR   SMR; Q02I11; -.
DR   CAZy; AA10; Auxiliary Activities 10.
DR   CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR   iPTMnet; Q02I11; -.
DR   PRIDE; Q02I11; -.
DR   EnsemblBacteria; ABJ10011; ABJ10011; PA14_53250.
DR   KEGG; pau:PA14_53250; -.
DR   HOGENOM; CLU_039396_2_0_6; -.
DR   OMA; MNHYMYD; -.
DR   BioCyc; PAER208963:G1G74-4481-MON; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR004302; Cellulose/chitin-bd_N.
DR   InterPro; IPR041029; GbpA_2.
DR   InterPro; IPR014756; Ig_E-set.
DR   Pfam; PF18416; GbpA_2; 1.
DR   Pfam; PF03067; LPMO_10; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
PE   1: Evidence at protein level;
KW   Chitin-binding; Phosphoprotein; Secreted; Signal.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..389
FT                   /note="Chitin-binding protein CbpD"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000431399"
FT   DOMAIN          26..208
FT                   /note="Chitin-binding type-4"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         37
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:24965220"
FT   MOD_RES         210
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:24965220"
SQ   SEQUENCE   389 AA;  41960 MW;  B32F75FAF75B4732 CRC64;
     MKHYSATLAL LPLTLALFLP QAAHAHGSME TPPSRVYGCF LEGPENPKSA ACKAAVAAGG
     TQALYDWNGV NQGNANGNHQ AVVPDGQLCG AGKALFKGLN LARSDWPSTA IAPDASGNFQ
     FVYKASAPHA TRYFDFYITK DGYNPEKPLA WSDLEPAPFC SITSVKLENG TYRMNCPLPQ
     GKTGKHVIYN VWQRSDSPEA FYACIDVSFS GAVANPWQAL GNLRAQQDLP AGATVTLRLF
     DAQGRDAQRH SLTLAQGNNG AKQWPLALAQ KVNQDSTLVN IGVLDAYGAV SPVASSQDNQ
     VYVRQAGYRF QVDIELPVEG GGEQPGGDGK VDFDYPQGLQ QYDAGTVVRG ADGKRYQCKP
     YPNSGWCKGW DLYYAPGKGM AWQDAWTLL