ID Q5L931_BACFN Unreviewed; 530 AA.
AC Q5L931; A0A380YSP5;
DT 21-JUN-2005, integrated into UniProtKB/TrEMBL.
DT 21-JUN-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Exported sulfatase {ECO:0000313|EMBL:CAH09401.1};
GN ORFNames=BF9343_3620 {ECO:0000313|EMBL:CAH09401.1};
OS Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019
OS / NCTC 9343 / Onslow).
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=272559 {ECO:0000313|EMBL:CAH09401.1, ECO:0000313|Proteomes:UP000006731};
RN [1] {ECO:0000313|EMBL:CAH09401.1, ECO:0000313|Proteomes:UP000006731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / NCTC 9343 /
RC Onslow {ECO:0000313|Proteomes:UP000006731};
RX PubMed=15746427; DOI=10.1126/science.1107008;
RA Cerdeno-Tarraga A.-M., Patrick S., Crossman L.C., Blakely G., Abratt V.,
RA Lennard N., Poxton I., Duerden B., Harris B., Quail M.A., Barron A.,
RA Clark L., Corton C., Doggett J., Holden M.T.G., Larke N., Line A., Lord A.,
RA Norbertczak H., Ormond D., Price C., Rabbinowitsch E., Woodward J.,
RA Barrell B.G., Parkhill J.;
RT "Extensive DNA inversions in the B. fragilis genome control variable gene
RT expression.";
RL Science 307:1463-1465(2005).
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; CR626927; CAH09401.1; -; Genomic_DNA.
DR RefSeq; WP_010993544.1; NZ_UFTH01000001.1.
DR PaxDb; 272559-BF9343_3620; -.
DR KEGG; bfs:BF9343_3620; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_10_4_10; -.
DR BioCyc; BFRA272559:G1GHZ-3957-MONOMER; -.
DR Proteomes; UP000006731; Chromosome.
DR GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-EC.
DR CDD; cd16144; ARS_like; 1.
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; PS00149; SULFATASE_2; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000006731};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..530
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5041159137"
FT DOMAIN 29..376
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT REGION 511..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000256|PIRSR:PIRSR600917-52"
SQ SEQUENCE 530 AA; 59178 MW; 76698E466ADF755B CRC64;
MKFVTLSLLA TALTVGGNAA EQARSSKQPN ILFILADDFG WRDLACTGSR YYESPNIDGI
ARNGVRFTQG YAACQVSSPS RASIMTGKFT ARHGITNWIG EGSGEEWRKM GRHSKLLPAQ
YVWQLPKEDI TLPEALKAHG YKTFMAGKWH LGGEGSYPED HGFDINIGGH EAGGPYPGGY
FAPYGNPKMK EGPDGENLSM RLAHETASFI ETHTRRNKKQ PFFAFLSFYA VHAPIETTEA
KWRHFRNKAD SMGIAPMGFE VDRTLPVRLQ QDNPIYAGLI QQMDDAVGVV LAKLHELGLD
ENTIIVFTSD NGGVSSGDAY ATSNYPLRGG KGRQWEGGIR VPLFIDFPGN TLKGDSCVVP
VTGADLYPTF LDMAGIPLMP GQHQDGVSLL PLLQGKSIPE RALYWHYPHY GNQGGEPSSI
IRQGDWKLIH YYEDGRDELY NLRIDETESE PLNVQYPEKV EFLSKKLSVW LTEVGARYPE
LDPQYNPVAE ALYKKKTRER MMKTLEATRK KQLGKDFKPN ADWWGSETKD
//
