ID   A0A2C6CQ32_9BACT        Unreviewed;       851 AA.
AC   A0A2C6CQ32;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Secretion system C-terminal sorting domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CEQ90_17860 {ECO:0000313|EMBL:PHI18481.1};
OS   Lewinellaceae bacterium SD302.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae.
OX   NCBI_TaxID=2014804 {ECO:0000313|EMBL:PHI18481.1, ECO:0000313|Proteomes:UP000223945};
RN   [1] {ECO:0000313|EMBL:PHI18481.1, ECO:0000313|Proteomes:UP000223945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD302 {ECO:0000313|EMBL:PHI18481.1,
RC   ECO:0000313|Proteomes:UP000223945};
RA   Wang K.;
RT   "The draft genome sequence of Lewinellaceae bacterium SD302.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 74 family.
CC       {ECO:0000256|ARBA:ARBA00037986}.
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:PHI18481.1}.
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DR   EMBL; PDLQ01000037; PHI18481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C6CQ32; -.
DR   OrthoDB; 9757947at2; -.
DR   Proteomes; UP000223945; Unassembled WGS sequence.
DR   GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd15482; Sialidase_non-viral; 1.
DR   Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 4.
DR   InterPro; IPR026444; Secre_tail.
DR   InterPro; IPR036278; Sialidase_sf.
DR   InterPro; IPR031778; Sortilin_N.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR   PANTHER; PTHR43739; XYLOGLUCANASE (EUROFUNG); 1.
DR   PANTHER; PTHR43739:SF2; XYLOGLUCANASE (EUROFUNG); 1.
DR   Pfam; PF18962; Por_Secre_tail; 1.
DR   Pfam; PF15902; Sortilin-Vps10; 1.
DR   SUPFAM; SSF110296; Oligoxyloglucan reducing end-specific cellobiohydrolase; 2.
DR   SUPFAM; SSF50939; Sialidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023326};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223945};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..851
FT                   /note="Secretion system C-terminal sorting domain-
FT                   containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013265349"
FT   DOMAIN          230..347
FT                   /note="Sortilin N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF15902"
FT   DOMAIN          773..850
FT                   /note="Secretion system C-terminal sorting"
FT                   /evidence="ECO:0000259|Pfam:PF18962"
SQ   SEQUENCE   851 AA;  91447 MW;  13A85F15A50C020E CRC64;
     MLSPLKLCLA LALLSILSAC EKQAEEKLAN ADKVSGAYEA LNFMGERLNY PESEMPKGAF
     TDAWRQHLTL QNNGGGRGGT ETWETMGPVN RAGRALSLAF NPQNANTLWL GTASGGLWRS
     HTEGLGGDAW EYVPTGFPVL GVSTIAFAPG DSTTMYIGTG EVYNYQAAGT GAAYRSTRGS
     YGMGILKSTD GGENWEMSLD WSYDQNRGIW MIKVHPNDPQ IVYAATTNGV YRTMNGGNDW
     EEVLSATMVT DLVIHPESPD SIVVGVGNLG SPGRGIFRST DGGDNWDQIT ENIPPDFQGK
     IQLNFAPSEP DILYASIGNG FSSAEGATWL CRSTDFGASW TVVNQTDYSL WQGWFSHDVD
     VSATDPDHIV AIGITTWRST DGGQNLIYET DGGIGPSNPD PADNTPGNVV HSDCHDVQFH
     PTNPDIVYVV SDGGVHRSTD GGQTFAFANG GLQTCQFYNG FSTAVTDESI AMGGLQDNGT
     ILWNGDDTWT VILGGDGSWS AINPVDPSIY YGSSQRLNVL RNTPGFGWEN MDIDQIGSAA
     FIAPYVISAT NGNILYAGHG GVSKTLNGGD SWSITNGGAS LDGNPVLSME VASNPDVVYA
     ATAPTTIFGG TRSGLFVTED GGNSWSERTG ILPDRYPMDI TVDPTNEAIA YVTFSGFGSG
     HVYKTLDYGE NWIDISGDLP DLPTNAVIVD PLYPDHVYIG NDFGVYASLD GGETWEGFQE
     GLYDAVMVFD LKISPTNRKL RAATHGNGAF QRDLVEPATG TQNIAASLPE VSIFPNPARE
     QTNLRFRLTD TRQLNIRLLD LQGRVIRQLA TETFANGEHS LPIPVTDLAS GNYFLQIQGS
     FGVHVEKLLV E
//