CBPD_PSEAE
ID CBPD_PSEAE Reviewed; 389 AA.
AC Q9I589; Q9RMI4;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Chitin-binding protein CbpD {ECO:0000303|PubMed:10671445};
DE AltName: Full=Protease LasD;
DE Flags: Precursor;
GN Name=cbpD {ECO:0000303|PubMed:10671445};
GN Synonyms=lasD {ECO:0000303|PubMed:7565088}; OrderedLocusNames=PA0852;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION,
RP PROTEOLYTIC CLEAVAGE, AND DISRUPTION PHENOTYPE.
RC STRAIN=PAO1 / PAO25;
RX PubMed=10671445; DOI=10.1128/jb.182.5.1257-1263.2000;
RA Folders J., Tommassen J., van Loon L.C., Bitter W.;
RT "Identification of a chitin-binding protein secreted by Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 182:1257-1263(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP PROTEIN SEQUENCE OF 26-40, AND INCORRECT FUNCTION.
RX PubMed=7565088; DOI=10.1111/j.1365-2958.1995.tb02298.x;
RA Park S., Galloway D.R.;
RT "Purification and characterization of LasD: a second staphylolytic
RT proteinase produced by Pseudomonas aeruginosa.";
RL Mol. Microbiol. 16:263-270(1995).
RN [4]
RP PROTEIN SEQUENCE OF 26-35, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RC STRAIN=PAO1 / PAO25;
RX PubMed=9642203; DOI=10.1128/jb.180.13.3467-3469.1998;
RA Braun P., de Groot A., Bitter W., Tommassen J.;
RT "Secretion of elastinolytic enzymes and their propeptides by Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 180:3467-3469(1998).
RN [5]
RP INCORRECT FUNCTION.
RX PubMed=9721177; DOI=10.1006/abbi.1998.0787;
RA Park S., Galloway D.R.;
RT "Pseudomonas aeruginosa LasD processes the inactive LasA precursor to the
RT active protease form.";
RL Arch. Biochem. Biophys. 357:8-12(1998).
RN [6]
RP DISRUPTION PHENOTYPE.
RX PubMed=23509956; DOI=10.1021/la400554g;
RA Ovchinnikova E.S., Krom B.P., Harapanahalli A.K., Busscher H.J.,
RA van der Mei H.C.;
RT "Surface thermodynamic and adhesion force evaluation of the role of chitin-
RT binding protein in the physical interaction between Pseudomonas aeruginosa
RT and Candida albicans.";
RL Langmuir 29:4823-4829(2013).
CC -!- FUNCTION: Binds chitin but does not hydrolyze it, has no detectable
CC protease or staphylolytic activity. {ECO:0000269|PubMed:10671445}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10671445,
CC ECO:0000269|PubMed:9642203}. Note=Secreted in an Xcp-dependent fashion
CC (a type II secretion pathway). {ECO:0000269|PubMed:10671445,
CC ECO:0000269|PubMed:9642203}.
CC -!- PTM: Can be detected in the extracellular supernatant as a 43 kDa
CC protein and a 23 kDa protein, both proteins have the same N-terminus
CC (PubMed:9642203, PubMed:10671445). Only the larger protein binds
CC chitin, which may protect it from further processing and/or degradation
CC by elastase (lasB) (PubMed:10671445, PubMed:9642203). It is not clear
CC whether the short form is functional or a degradation product.
CC {ECO:0000269|PubMed:10671445, ECO:0000269|PubMed:9642203, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Decreases chitin-binding, has no visible effect
CC on extracellular staphylolytic or protease activity (PubMed:10671445).
CC Decreased association with the hyphae form of C.albicans strain SC5314;
CC P.aeruginosa does not adhere to yeast form C.albicans
CC (PubMed:23509956). {ECO:0000269|PubMed:10671445,
CC ECO:0000269|PubMed:23509956}.
CC -!- CAUTION: Was originally thought to be a protease that processes pro-
CC LasA. {ECO:0000269|PubMed:7565088, ECO:0000269|PubMed:9721177}.
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DR EMBL; AF196565; AAF12807.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04241.1; -; Genomic_DNA.
DR PIR; F83538; F83538.
DR PIR; S67918; S67918.
DR RefSeq; NP_249543.1; NC_002516.2.
DR RefSeq; WP_003114231.1; NZ_QZGE01000007.1.
DR AlphaFoldDB; Q9I589; -.
DR SASBDB; Q9I589; -.
DR SMR; Q9I589; -.
DR STRING; 287.DR97_1092; -.
DR CAZy; AA10; Auxiliary Activities 10.
DR CAZy; CBM73; Carbohydrate-Binding Module Family 73.
DR PaxDb; Q9I589; -.
DR PRIDE; Q9I589; -.
DR EnsemblBacteria; AAG04241; AAG04241; PA0852.
DR GeneID; 877771; -.
DR KEGG; pae:PA0852; -.
DR PATRIC; fig|208964.12.peg.884; -.
DR PseudoCAP; PA0852; -.
DR HOGENOM; CLU_039396_2_0_6; -.
DR InParanoid; Q9I589; -.
DR OMA; MNHYMYD; -.
DR BioCyc; PAER208964:G1FZ6-867-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005615; C:extracellular space; IDA:PseudoCAP.
DR GO; GO:0008061; F:chitin binding; IDA:PseudoCAP.
DR GO; GO:0015628; P:protein secretion by the type II secretion system; IDA:PseudoCAP.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:PseudoCAP.
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; Direct protein sequencing; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:7565088,
FT ECO:0000269|PubMed:9642203"
FT CHAIN 26..389
FT /note="Chitin-binding protein CbpD"
FT /id="PRO_0000431398"
FT DOMAIN 26..208
FT /note="Chitin-binding type-4"
FT /evidence="ECO:0000255"
FT CONFLICT 305
FT /note="Q -> R (in Ref. 1; AAF12807)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 41917 MW; B32386FF9452D732 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 SLTLAQGANG AKQWPLALAQ KVNQDSTLVN IGVLDAYGAV SPVASSQDNQ
VYVRQAGYRF QVDIELPVEG GGEQPGGDGK VDFDYPQGLQ QYDAGTVVRG ADGKRYQCKP
YPNSGWCKGW DLYYAPGKGM AWQDAWTLL
