ID   F3NJS3_9ACTN            Unreviewed;       883 AA.
AC   F3NJS3;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Hydrolase {ECO:0000313|EMBL:EGG46334.1};
GN   ORFNames=SGM_3387 {ECO:0000313|EMBL:EGG46334.1};
OS   Streptomyces griseoaurantiacus M045.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG46334.1, ECO:0000313|Proteomes:UP000003022};
RN   [1] {ECO:0000313|EMBL:EGG46334.1, ECO:0000313|Proteomes:UP000003022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M045 {ECO:0000313|EMBL:EGG46334.1,
RC   ECO:0000313|Proteomes:UP000003022};
RX   PubMed=21551298; DOI=10.1128/JB.05053-11;
RA   Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT   "Draft genome sequence of the marine bacterium Streptomyces
RT   griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT   with a pABA core component.";
RL   J. Bacteriol. 193:3417-3418(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 2 family.
CC       {ECO:0000256|ARBA:ARBA00007401}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGG46334.1}.
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DR   EMBL; AEYX01000037; EGG46334.1; -; Genomic_DNA.
DR   RefSeq; WP_006141156.1; NZ_AEYX01000037.1.
DR   AlphaFoldDB; F3NJS3; -.
DR   STRING; 996637.SGM_3387; -.
DR   eggNOG; COG3250; Bacteria.
DR   Proteomes; UP000003022; Unassembled WGS sequence.
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; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 3.90.182.10; Toxin - Anthrax Protective Antigen;domain 1; 1.
DR   InterPro; IPR036156; Beta-gal/glucu_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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; IPR037524; PA14/GLEYA.
DR   InterPro; IPR011658; PA14_dom.
DR   InterPro; IPR006311; TAT_signal.
DR   PANTHER; PTHR42732; BETA-GALACTOSIDASE; 1.
DR   PANTHER; PTHR42732:SF2; BETA-MANNOSIDASE; 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   Pfam; PF07691; PA14; 1.
DR   SMART; SM00758; PA14; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF56988; Anthrax protective antigen; 1.
DR   SUPFAM; SSF49303; beta-Galactosidase/glucuronidase domain; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS51820; PA14; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGG46334.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003022};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..883
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5039624403"
FT   DOMAIN          47..191
FT                   /note="PA14"
FT                   /evidence="ECO:0000259|PROSITE:PS51820"
SQ   SEQUENCE   883 AA;  96162 MW;  B98A7FB46943692F CRC64;
     MRTRRLRDRL ALLLAAAMAA AGLAAATGPA AAVPADDGTR ATADSPAEAH GLKGEYYTQS
     AEGAFDFATL KATTFDPTLD FADLEPRLRA TTGQDNDVSA RWTGRLVPEK TGATTFSIIG
     DNGFRLWVDG HLVIDHWVDD WDKEQTGEAV DLTAGHAVDI KVEYFEHYGG SNLHVRWTPP
     GGSKTAIPQS AFRLPEGYDY DGPVATTVRP DGRTLQLDFP SPLAGVPAGL TDHLSAVVGG
     ATWPLGKAKL DRKDPSSLLI ALDQPVVGNK TGTAKGTADV RYDGKGGLAT TDGKDTHTVG
     AFWTSGGNKS TYELTTKWAK QVGPHNALPE YPRPQLTRTT WQNLNGRWQF AAATEGERPP
     VGRTLGEHIL VPYPVESQLS GLERHEERMW YRRTFTVPKN WHVGSKQRLQ LNFGAVDWRA
     EVYVNGTKVA EHQGGYDKFS ADVTKALKPG RTQELIVGVY DPTDSASGPN QPMGKQRLDP
     SGIWYTPSSG IWQTVWMEPV AADHVDNLKL TPDVDKSTLT IDPQGVREGL KVTATAYAGK
     RAVGTVTGRT GRPLTLHLRD PHLWSPDDPY LYQLKVRVGS DSVGSYFGMR SVAVKNVNGT
     PRTLLNGKPI FLMATLDQGF WPDGLHTAPT DEALAHDLKV HKQLGFNSVR KHIKVEPDRW
     FYWADKLGLM VWQDMPAMNA GTSPSTAARA EYERELKQMI DEHISSPSVV MWVTFNEGWG
     QYDMARIADQ AKAWDPTRLV NSMSGINLGA DGGTGDIIDE HGYPSPALPP HPDGRRALVS
     GEYGGLGLAV PGHAWSVQQS YVDVDPSTYT DDYLTKLDEV HALACKGGNG AVYTQISDVE
     GELNGLLTYD RRVLKPDADR VRAAQRSLIH DASQPVVAGC DGN
//