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Database: UniProt
Entry: A4X9B3_SALTO
LinkDB: A4X9B3_SALTO
Original site: A4X9B3_SALTO 
ID   A4X9B3_SALTO            Unreviewed;       360 AA.
AC   A4X9B3;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Chitin-binding, domain 3 protein {ECO:0000313|EMBL:ABP55474.1};
GN   OrderedLocusNames=Strop_3037 {ECO:0000313|EMBL:ABP55474.1};
OS   Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / JCM 13857 / NBRC
OS   105044 / CNB-440).
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Salinispora.
OX   NCBI_TaxID=369723 {ECO:0000313|EMBL:ABP55474.1, ECO:0000313|Proteomes:UP000000235};
RN   [1] {ECO:0000313|Proteomes:UP000000235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-916 / DSM 44818 / CNB-440
RC   {ECO:0000313|Proteomes:UP000000235};
RX   PubMed=17563368; DOI=10.1073/pnas.0700962104;
RA   Udwary D.W., Zeigler L., Asolkar R.N., Singan V., Lapidus A., Fenical W.,
RA   Jensen P.R., Moore B.S.;
RT   "Genome sequencing reveals complex secondary metabolome in the marine
RT   actinomycete Salinispora tropica.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:10376-10381(2007).
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DR   EMBL; CP000667; ABP55474.1; -; Genomic_DNA.
DR   RefSeq; WP_012014252.1; NC_009380.1.
DR   AlphaFoldDB; A4X9B3; -.
DR   STRING; 369723.Strop_3037; -.
DR   CAZy; AA10; Auxiliary Activities 10.
DR   CAZy; CBM2; Carbohydrate-Binding Module Family 2.
DR   KEGG; stp:Strop_3037; -.
DR   PATRIC; fig|369723.5.peg.3126; -.
DR   eggNOG; COG3397; Bacteria.
DR   HOGENOM; CLU_063855_0_0_11; -.
DR   Proteomes; UP000000235; Chromosome.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd21177; LPMO_AA10; 1.
DR   Gene3D; 2.60.40.290; -; 1.
DR   Gene3D; 2.70.50.50; chitin-binding protein cbp21; 1.
DR   InterPro; IPR001919; CBD2.
DR   InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
DR   InterPro; IPR012291; CBM2_carb-bd_dom_sf.
DR   InterPro; IPR004302; Cellulose/chitin-bd_N.
DR   InterPro; IPR014756; Ig_E-set.
DR   PANTHER; PTHR34823:SF1; CHITIN-BINDING TYPE-4 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34823; GLCNAC-BINDING PROTEIN A; 1.
DR   Pfam; PF00553; CBM_2; 1.
DR   Pfam; PF03067; LPMO_10; 1.
DR   SMART; SM00637; CBD_II; 1.
DR   SUPFAM; SSF49384; Carbohydrate-binding domain; 1.
DR   SUPFAM; SSF81296; E set domains; 1.
DR   PROSITE; PS51173; CBM2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000000235};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..360
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038856596"
FT   DOMAIN          256..360
FT                   /note="CBM2"
FT                   /evidence="ECO:0000259|PROSITE:PS51173"
FT   REGION          230..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..259
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   360 AA;  37983 MW;  57A1E8AE78ECBD74 CRC64;
     MSSYRARTAA LLTAATTLLA AAAVLTVRSE PAAAHGAAMV PGSRTFLCWQ DGLSPTGEIQ
     PYNPACSAAV DQSGANSLYN WFSVLRSDAD GRTVGFIPDG QLCSGGNPGF LGYDLARIDW
     PLTHLTAGQN IEFRYSNWAH HPGTFYFYVT KDSWSPTRPL AWSDLEEQPF LTVTNPPQRG
     GPGTDDGHYY FAGTLPADKS GRHLIYSRWV RSDSPENFFG CSDVTFDGGN GEVTGIGPGG
     TAPPPSPTTA PPSPTTPPPS GDCMAVYKVI NAWPGGFQGE VEIMNHAATT WAGWTARWTW
     PSGQSIVQLW SGTHTTSGSA VAVTNASYNG TLAPGSRATF GFLASLSGTN TSPTVTCTGS
//
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