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Database: UniProt
Entry: A0A1M4SID9_9BACE
LinkDB: A0A1M4SID9_9BACE
Original site: A0A1M4SID9_9BACE 
ID   A0A1M4SID9_9BACE        Unreviewed;       457 AA.
AC   A0A1M4SID9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Arylsulfatase A {ECO:0000313|EMBL:SHE31918.1};
GN   ORFNames=SAMN05444405_101108 {ECO:0000313|EMBL:SHE31918.1};
OS   Bacteroides luti.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=1297750 {ECO:0000313|EMBL:SHE31918.1, ECO:0000313|Proteomes:UP000184509};
RN   [1] {ECO:0000313|EMBL:SHE31918.1, ECO:0000313|Proteomes:UP000184509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26991 {ECO:0000313|EMBL:SHE31918.1,
RC   ECO:0000313|Proteomes:UP000184509};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PTM: The conversion to 3-oxoalanine (also known as C-formylglycine,
CC       FGly), of a serine or cysteine residue in prokaryotes and of a cysteine
CC       residue in eukaryotes, is critical for catalytic activity.
CC       {ECO:0000256|PIRSR:PIRSR600917-52}.
CC   -!- SIMILARITY: Belongs to the sulfatase family.
CC       {ECO:0000256|ARBA:ARBA00008779}.
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DR   EMBL; FQTV01000001; SHE31918.1; -; Genomic_DNA.
DR   RefSeq; WP_073398570.1; NZ_FQTV01000001.1.
DR   AlphaFoldDB; A0A1M4SID9; -.
DR   STRING; 1297750.SAMN05444405_101108; -.
DR   OrthoDB; 9765065at2; -.
DR   Proteomes; UP000184509; Unassembled WGS sequence.
DR   GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:UniProt.
DR   Gene3D; 3.30.1120.10; -; 1.
DR   Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR   InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR   InterPro; IPR024607; Sulfatase_CS.
DR   InterPro; IPR000917; Sulfatase_N.
DR   PANTHER; PTHR42693:SF33; ARYLSULFATASE; 1.
DR   PANTHER; PTHR42693; ARYLSULFATASE FAMILY MEMBER; 1.
DR   Pfam; PF00884; Sulfatase; 1.
DR   SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
DR   PROSITE; PS00523; SULFATASE_1; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184509};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..457
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012499695"
FT   DOMAIN          30..357
FT                   /note="Sulfatase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00884"
FT   MOD_RES         78
FT                   /note="3-oxoalanine (Ser)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600917-52"
SQ   SEQUENCE   457 AA;  50912 MW;  1554E8540E243DDD CRC64;
     MKPLIKTVPA LLGGLSFFTA AHAQQESKRP NIIFILADDM GYGDLACYGN KVVKTPNIDK
     LASDGIRFTN CYAGSAISSP SRCSLLTGKH TGHTTIRDNF CKAGGLPGLK GTTPIRRMHL
     LPNDTTIATV LGSAGYRTCL VNKWHQDGFN PGAGPLDRGF DEFYGWLIST ENSNTPYYYP
     ALRFYNRDLK VIPENENNKR GIHDSDLSVN ESIDFIDRNK NNPFFLYLAF DVPHEPYFIN
     SLEPYTNSSL SDTGKLYASL ITHTDEAIGR LIDHLDKTGL RDNTIIIFAS DNGGAVMAPL
     EELNCNAGFR GRKGILYEGG IKVPFIVNCP KHIKGGQTMK NLIYFPDVMP TLADYAHAKL
     PQHIDGVSIK ALLDGKKQDT DNRVFYWEFP GNQVAVRKGD WKIVSVKKGT KLELYNITKD
     PYEKTNLAEK YPEVLKDLEK EIKKSHVASP NWPLEGE
//
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