ID A0A0G3GW68_9CORY Unreviewed; 467 AA.
AC A0A0G3GW68;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=GA module {ECO:0000313|EMBL:AKK05426.1};
GN ORFNames=CMUST_05445 {ECO:0000313|EMBL:AKK05426.1};
OS Corynebacterium mustelae.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=571915 {ECO:0000313|EMBL:AKK05426.1, ECO:0000313|Proteomes:UP000035199};
RN [1] {ECO:0000313|EMBL:AKK05426.1, ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|EMBL:AKK05426.1,
RC ECO:0000313|Proteomes:UP000035199};
RX PubMed=26358597;
RA Ruckert C., Eimer J., Winkler A., Tauch A.;
RT "Complete Genome Sequence of the Type Strain Corynebacterium mustelae DSM
RT 45274, Isolated from Various Tissues of a Male Ferret with Lethal Sepsis.";
RL Genome Announc. 3:e01012-15(2015).
RN [2] {ECO:0000313|Proteomes:UP000035199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45274 {ECO:0000313|Proteomes:UP000035199};
RA Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT "Complete genome sequence of Corynebacterium mustelae DSM 45274, isolated
RT from various tissues of a male ferret with lethal sepsis.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011542; AKK05426.1; -; Genomic_DNA.
DR RefSeq; WP_052844544.1; NZ_CP011542.1.
DR AlphaFoldDB; A0A0G3GW68; -.
DR STRING; 571915.CMUST_05445; -.
DR KEGG; cmv:CMUST_05445; -.
DR PATRIC; fig|571915.4.peg.1155; -.
DR OrthoDB; 7183084at2; -.
DR Proteomes; UP000035199; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 1.20.5.420; Immunoglobulin FC, subunit C; 1.
DR InterPro; IPR020840; Extracell_matrix-bd_GA.
DR InterPro; IPR002988; GA_module.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR009063; Ig/albumin-bd_sf.
DR Pfam; PF01468; GA; 1.
DR SMART; SM00844; GA; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF46997; Bacterial immunoglobulin/albumin-binding domains; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000035199};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..467
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005184333"
FT TRANSMEM 441..464
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..340
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..422
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 467 AA; 51504 MW; 366D866AA3B1B191 CRC64;
MRLHHALGSL ITATGLALSA VAAPADASPT SLPLPEHKGF HPDAGERSDC EPIVTAYYRT
WRDKEIQQLP DDRVGPNVIA MTDIPHNIDV LSLIHVPDHQ QSDQQFWATF ASTYLPELHR
RGTKVLYTLD ISAVLDPSLK PTSSPEEYAA HAQRLVDKYV RPHKLDGLDI DMERDLSFDQ
RIVLRNTMRA LTQLVGPFSN TNTLLTYNTN RNAQKAYIDE VAQYVNYVFV QTYSVTDPNE
IQYSYWNTYR FYLSSCQFLP SYANPEEFDR NRFLGAIGPV EETAAVKIAG WQPFQGGVKG
GIMTYAIDRD GMTYDQPDIS TLRVTTFPVI KRVTAVLKAK KFAAAKETAA QTVTNLTNLT
ETQRQTYIQN INAALTFEDV EALVKAAREH PAAPTATTTP TATSTTSTTP TISSSTNETT
SAPTPPQPEP RDRPSSSLTG LYAAIAAIVA AVLGGIAALV FQFFGRL
//
