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Database: UniProt
Entry: D7C4S5_STRBB
LinkDB: D7C4S5_STRBB
Original site: D7C4S5_STRBB 
ID   D7C4S5_STRBB            Unreviewed;       914 AA.
AC   D7C4S5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=alpha-L-rhamnosidase {ECO:0000256|ARBA:ARBA00012652};
DE            EC=3.2.1.40 {ECO:0000256|ARBA:ARBA00012652};
GN   OrderedLocusNames=SBI_03005 {ECO:0000313|EMBL:ADI06126.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI06126.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI06126.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI06126.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of terminal non-reducing alpha-L-rhamnose residues
CC         in alpha-L-rhamnosides.; EC=3.2.1.40;
CC         Evidence={ECO:0000256|ARBA:ARBA00001445};
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DR   EMBL; CP002047; ADI06126.1; -; Genomic_DNA.
DR   AlphaFoldDB; D7C4S5; -.
DR   STRING; 749414.SBI_03005; -.
DR   CAZy; GH78; Glycoside Hydrolase Family 78.
DR   KEGG; sbh:SBI_03005; -.
DR   PATRIC; fig|749414.3.peg.3113; -.
DR   eggNOG; COG3387; Bacteria.
DR   HOGENOM; CLU_002926_1_1_11; -.
DR   Proteomes; UP000000377; Chromosome.
DR   GO; GO:0030596; F:alpha-L-rhamnosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR035396; Bac_rhamnosid6H.
DR   InterPro; IPR035398; Bac_rhamnosid_C.
DR   InterPro; IPR013737; Bac_rhamnosid_N.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008902; Rhamnosid_concanavalin.
DR   PANTHER; PTHR33307:SF11; ALPHA-L-RHAMNOSIDASE; 1.
DR   PANTHER; PTHR33307; ALPHA-RHAMNOSIDASE (EUROFUNG); 1.
DR   Pfam; PF05592; Bac_rhamnosid; 1.
DR   Pfam; PF17389; Bac_rhamnosid6H; 1.
DR   Pfam; PF17390; Bac_rhamnosid_C; 1.
DR   Pfam; PF08531; Bac_rhamnosid_N; 1.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..914
FT                   /note="alpha-L-rhamnosidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003093995"
FT   DOMAIN          173..320
FT                   /note="Bacterial alpha-L-rhamnosidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08531"
FT   DOMAIN          349..448
FT                   /note="Alpha-L-rhamnosidase concanavalin-like"
FT                   /evidence="ECO:0000259|Pfam:PF05592"
FT   DOMAIN          457..794
FT                   /note="Alpha-L-rhamnosidase six-hairpin glycosidase"
FT                   /evidence="ECO:0000259|Pfam:PF17389"
FT   DOMAIN          816..874
FT                   /note="Alpha-L-rhamnosidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17390"
SQ   SEQUENCE   914 AA;  98418 MW;  DB954D58CADBF2DF CRC64;
     MLLAAALLPV VSTAAPGHAA AAEPRGGHAP LAPADLTVGD RARPLDVEGA PLFGWRPRDV
     DPGERQTAYQ IRVARTGAGP GGSRQVWDSG KVVSARQAYV AYDGPDLPGG TGYTWTVRTW
     DRTGAASPWA ARAAFDTGIS DATWQASWIR RTTGDKDDYT LARKEFTVGA SPVVRARLYV
     AASQQYRAYV NGRLVDRGAA YAYPDEGYYQ AGDVTRDLKA GRPAAIGVLA HWYGPGQGRP
     AGEPGLLARL VVEHADGSRQ VVVSDGSWRV ARGPWLSLPY RNDDGRDYIE GVDGRTVQRQ
     RGWNRPGFDA SSWQSPQVVG VHPAGGFSHL RSQQTRLAYR TVRPVTVTRL DSGAVVADFG
     TIIPAVPQVR FARGVSGRTI DMRAGYVRNA DGTVSDSAHD NQKTDLSYQY IQHDGAQTFQ
     AYTYEGFRYL QIDDPGEPLS ASSIAAVVQH TDADPARAAT FRSSDPTLDA VAELMRRSAL
     YDSQEQFLDT PTREKGQFLG DSVDVSRALM AGSGDRALTA RAIREFAESQ QRYWPDGRMN
     AVYPNGDGKR DIPDYTEMFP GWVWEYYLNS GDRATLAATY PASAAVADYI RRYIDPATGL
     VTKLAGGSGA YQYGIIDWPN RYGYDTDTTA RTTVNILAVD ALRRTADQAA ALGRPKAEAD
     ALRADAAKLA EAVNDRLRRP DSLYTDGLKA DGTQSAHASQ IANAYAVAFG IAPEGSVDTI
     ADHLVSLKLQ MGPMTANWLL TALHRAGRDD QVLARITDRT SLGWANILAR GGTFTWESWE
     APDDGQSLSH GWGATALVDL QQDLLGLNVT GTAATTLRIR PPRDTELTHA EGTVWTQAGT
     VGVRWNTTAH GTQVKVDIPV NVTAEVEVPL ADGRVPKASG AGPDGASAPR FEGVRNGRAI
     YMVGSGHSTF TPAV
//
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