ID D7ID33_9BACE Unreviewed; 482 AA.
AC D7ID33;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Sulfatase family protein {ECO:0000313|EMBL:EFI04537.1};
GN ORFNames=HMPREF9007_02205 {ECO:0000313|EMBL:EFI04537.1};
OS Bacteroides sp. 1_1_14.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=469585 {ECO:0000313|EMBL:EFI04537.1, ECO:0000313|Proteomes:UP000003951};
RN [1] {ECO:0000313|EMBL:EFI04537.1, ECO:0000313|Proteomes:UP000003951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_1_14 {ECO:0000313|EMBL:EFI04537.1,
RC ECO:0000313|Proteomes:UP000003951};
RG The Broad Institute Genome Sequencing Platform;
RA Ward D., Earl A., Feldgarden M., Gevers D., Young S.K., Zeng Q.,
RA Koehrsen M., Alvarado L., Berlin A., Bochicchio J., Borenstein D.,
RA Chapman S.B., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA Griggs A., Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA Larson L., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T., Walk T., White J.,
RA Yandava C., Strauss J., Daigneault M., McDonald J., Ambrose C.E.,
RA Allen-Vercoe E., Haas B., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacteroides sp. strain 1_1_14.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG774705; EFI04537.1; -; Genomic_DNA.
DR AlphaFoldDB; D7ID33; -.
DR HOGENOM; CLU_006332_9_0_10; -.
DR Proteomes; UP000003951; Unassembled WGS sequence.
DR GO; GO:0004423; F:iduronate-2-sulfatase activity; IEA:InterPro.
DR CDD; cd16030; iduronate-2-sulfatase; 1.
DR Gene3D; 3.40.720.10; Alkaline Phosphatase, subunit A; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR035874; IDS.
DR InterPro; IPR000917; Sulfatase_N.
DR PANTHER; PTHR45953; IDURONATE 2-SULFATASE; 1.
DR PANTHER; PTHR45953:SF1; IDURONATE 2-SULFATASE; 1.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; Alkaline phosphatase-like; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..482
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003097419"
FT DOMAIN 36..383
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT MOD_RES 82
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000256|PIRSR:PIRSR600917-52"
SQ SEQUENCE 482 AA; 54831 MW; 03B341C62D637F85 CRC64;
MKNAISVKYT LLCGTACCMV SAVQAQHNVS DVSRMNVLFL MADDMRPELG CYGVEAVKTP
NMDRLASSGV LFQNAYCNVP VSGASRASLL TGVYPHYPDR FVNFSAYASK DCPEAIPLSG
WFTKNGYHTV SDGKVFHHMS DHAASWSEPP YRNHPDGYDV YWAEYNKWEL WMNSESGKTI
NPKTMRGPFC ESADVPDTAY DDGKLAERAI RDLRRMKEMN KPFFLACGFW KPHLPFNAPK
KYWDLYKREE IPLASNRFRP EGLPEQVRNS SEIYAYARVT DTGDADFQRE VKHGYYACLS
YVDAQIGKVL DALDELGLAE NTIVVLLGDH GWNLGEHDFV GKHNLMDRST HVPLIIRVPG
MKKGKTWSMV EFVDLYPTLC ELCQIPQPAE QLDGQSFAKV FSNLKAKTKD EVYIQWEGGD
NAVDQRFSYA EWMKGDVKKA SMLFDHRIDK EENKNRVNEK KYKSKVESLS SFIKVKKSSL
KK
//
