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
//