ID F3ZSL3_9BACE Unreviewed; 466 AA.
AC F3ZSL3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Sulfatase {ECO:0000313|EMBL:EGJ72165.1};
GN ORFNames=Bcop_1990 {ECO:0000313|EMBL:EGJ72165.1};
OS Bacteroides coprosuis DSM 18011.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=679937 {ECO:0000313|EMBL:EGJ72165.1, ECO:0000313|Proteomes:UP000018439};
RN [1] {ECO:0000313|EMBL:EGJ72165.1, ECO:0000313|Proteomes:UP000018439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18011 {ECO:0000313|EMBL:EGJ72165.1,
RC ECO:0000313|Proteomes:UP000018439};
RX PubMed=21677860; DOI=10.4056/sigs.1784330;
RA Land M., Held B., Gronow S., Abt B., Lucas S., Del Rio T.G., Nolan M.,
RA Tice H., Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Hauser L., Brambilla E.M., Rohde M., Goker M.,
RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Lapidus A.;
RT "Non-contiguous finished genome sequence of Bacteroides coprosuis type
RT strain (PC139).";
RL Stand. Genomic Sci. 4:233-243(2011).
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; CM001167; EGJ72165.1; -; Genomic_DNA.
DR RefSeq; WP_006745321.1; NZ_CM001167.1.
DR AlphaFoldDB; F3ZSL3; -.
DR STRING; 679937.Bcop_1990; -.
DR eggNOG; COG3119; Bacteria.
DR HOGENOM; CLU_006332_9_2_10; -.
DR OrthoDB; 9762324at2; -.
DR Proteomes; UP000018439; Chromosome.
DR GO; GO:0008484; F:sulfuric ester hydrolase activity; IEA:UniProt.
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:UP000018439};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..466
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003304001"
FT DOMAIN 35..350
FT /note="Sulfatase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00884"
FT MOD_RES 83
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000256|PIRSR:PIRSR600917-52"
SQ SEQUENCE 466 AA; 52696 MW; FA56554D8D3CB4DA CRC64;
MTNTSKLLSI MVGGASLLQV APAMAKPKAE KQTQPNIILI MTDQHTANAL SCAGNPYVST
PGIDGLAQDG IRFTRAYASY PLSGPSRASM ITGKMPVQLG VKDNSVGDIS AEELANSMGN
VAKNAGYECL YAGKWHAPLE INLPEEGTGF TKVCDMDDRV LVEKSKPFLE KKYDKPLFYV
ASFLNPHETC EFAREEALHY GKLDIDKEKD NYPPLPMNAS IPAYYPEAIT LHRHFVPRSY
PTERYTDDDW RKYIYAYYRF VERVDKEIVK LVDVLKSNDL YENSLIIFMS DHGDGVGAHR
ANQKRVLQEE IANVPFIVKP PKSKFKGEVN ETALISTNLD LYQTICDITG AGENHDQRFG
KSIRPLIEGK TIKHHDEVYV ETFLDGVETR GWAVIGEKHK YVVYRQFKNA EQLFNLENDP
LEMQNLAPVK AYDEIKQEMR AKLYDWAVKT DDKMLRRVTS NCDDVN
//
