ID A0A0H4CB49_9ACTN Unreviewed; 1030 AA.
AC A0A0H4CB49;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Beta-galactosidase {ECO:0000313|EMBL:AKN74353.1};
GN ORFNames=QR97_35605 {ECO:0000313|EMBL:AKN74353.1};
OS Streptomyces sp. PBH53.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1577075 {ECO:0000313|EMBL:AKN74353.1, ECO:0000313|Proteomes:UP000036399};
RN [1] {ECO:0000313|EMBL:AKN74353.1, ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|EMBL:AKN74353.1,
RC ECO:0000313|Proteomes:UP000036399};
RX PubMed=26227608;
RA Gosse J.T., Hill P., Dowd S.E., Boddy C.N.;
RT "Draft Genome Sequence of Streptomyces sp. Strain PBH53, Isolated from an
RT Urban Environment.";
RL Genome Announc. 3:e00859-e00815(2015).
RN [2] {ECO:0000313|Proteomes:UP000036399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBH53 {ECO:0000313|Proteomes:UP000036399};
RA Gosse J.T., Boddy C.N., Hill P.B.;
RT "Draft Genome Sequence of Streptomyces sp. strain PBH53, isolated from
RT urban environment.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC {ECO:0000256|ARBA:ARBA00007401}.
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DR EMBL; CP011799; AKN74353.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H4CB49; -.
DR STRING; 1577075.QR97_35605; -.
DR PATRIC; fig|1577075.3.peg.7470; -.
DR Proteomes; UP000036399; Chromosome.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR InterPro; IPR032311; DUF4982.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR040605; Glyco_hydro2_dom5.
DR InterPro; IPR006101; Glyco_hydro_2.
DR InterPro; IPR006103; Glyco_hydro_2_cat.
DR InterPro; IPR006102; Glyco_hydro_2_Ig-like.
DR InterPro; IPR006104; Glyco_hydro_2_N.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR PANTHER; PTHR42732:SF1; BETA-MANNOSIDASE; 1.
DR Pfam; PF16355; DUF4982; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF18565; Glyco_hydro2_C5; 1.
DR Pfam; PF00703; Glyco_hydro_2; 1.
DR Pfam; PF02836; Glyco_hydro_2_C; 1.
DR Pfam; PF02837; Glyco_hydro_2_N; 1.
DR PRINTS; PR00132; GLHYDRLASE2.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000036399};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..31
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 32..1030
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005205278"
FT DOMAIN 49..205
FT /note="Glycosyl hydrolases family 2 sugar binding"
FT /evidence="ECO:0000259|Pfam:PF02837"
FT DOMAIN 215..318
FT /note="Glycoside hydrolase family 2 immunoglobulin-like
FT beta-sandwich"
FT /evidence="ECO:0000259|Pfam:PF00703"
FT DOMAIN 325..479
FT /note="Glycoside hydrolase family 2 catalytic"
FT /evidence="ECO:0000259|Pfam:PF02836"
FT DOMAIN 650..746
FT /note="DUF4982"
FT /evidence="ECO:0000259|Pfam:PF16355"
FT DOMAIN 760..858
FT /note="Glycoside hydrolase family 2"
FT /evidence="ECO:0000259|Pfam:PF18565"
FT DOMAIN 901..1015
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|Pfam:PF00754"
FT REGION 532..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..884
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 111528 MW; C28A62EAC0638DB6 CRC64;
MTVTRRSVLV AATAAPATGT LLSIPAPAAH AAEASAAGGR HTVPLRDGWR FALVDPGGLT
DPTGAYARAA DPGHDDGDWR EVAVPHDWSI EQTPTTEHGT TSGTGFFPGG LGWYRLAFTL
PPAWAGKRVS VEFDGVYMDA YVHCNGTQVG HHPYGYTGFA LDLTDLVHTD GTTPNVLAVK
VQNQLPSSRW YSGSGIYREA RLVITEPVHV ARWGTYVTTP EISADRALVR VRTTVRNASG
AGAEVEIRSR ITDPDGRTVA RTAGTAYVAD EAAETHELTV PQPLLWDFAT PEHRYTLHTE
LRVGGRTTDT CRTSFGIRTF RFDPDEGFSL NGSHTKIKGV DLHHDQGALG AASSIDAVRR
QMRIMKSMGV NALRTSHNPP SPEMIRVCEE LGIVMMVEAF DCWRTGKTRY DYGRFFDEWC
ERDATEMVLA ARNSPAVLLW SIGNEIPDST STAGLAMADR IIGAIKAADA TRPLVIGSNK
YHSVPAAGSA ADRMLAKLDG LGLNYNTAKS VDALHATYPH LFLFESESSS ETSTRGTYQE
PEHLNTGENH TPGKREVSSY DNNLASWTMS GEYGHKKDRD RKWFAGQFLW SGIDYIGEPT
PYDVFPVKAS FFGAVDTAGF PKDMYHLFKS QWTTEPMVHL LPMSWNHREG ETVEVWAYAN
VPSVELFLDG KSLGVREFDV KRTTDGRTYL ETTEPTGDDK TFTDGPYPGS YTSPNGSAGK
LHLTWKVPFR PGELKAVARR DGRVVATDVL RTAGAPHAVR LTADRTSLAA DGRALAFVTA
EIVDAHGVVV PDAEHLIAFD VSGGSLAGVD NGRQESAERY QASTRTAFHG KALAIVRSGT
RAGTLKVTAR AAGLRPDTAR LRTTPARSAA TTAPAVFRPD HPAPPDYPWA DAGYSGRPDT
LPAAMLDGDP ATGWSNAFVK AATALLPAFR GARAEDWVSV DFGRTRTFDR VAVSFTVDAG
HTLPARVEVA VWDGHAHTPV TGARVDWADA SDSPTVITFD AVRGSRLRLT LTSAYPGEAK
GAVRISRLDL
//
