ATSA_KLEPN
ID ATSA_KLEPN Reviewed; 577 AA.
AC Q9X759;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Arylsulfatase;
DE Short=AS;
DE EC=3.1.6.1;
DE AltName: Full=Aryl-sulfate sulphohydrolase;
DE Flags: Precursor;
GN Name=atsA;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 10031 / DSM 681 / NBRC 3512 / NCIMB 9111 / NCTC 7427;
RX PubMed=10336424; DOI=10.1074/jbc.274.22.15375;
RA Szameit C., Miech C., Balleininger M., Schmidt B., von Figura K.,
RA Dierks T.;
RT "The iron sulfur protein AtsB is required for posttranslational formation
RT of formylglycine in the Klebsiella sulfatase.";
RL J. Biol. Chem. 274:15375-15381(1999).
RN [2]
RP PROTEIN SEQUENCE OF 63-76, OXOALANINE AT SER-72, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=ATCC 10031 / DSM 681 / NBRC 3512 / NCIMB 9111 / NCTC 7427;
RX PubMed=9478923; DOI=10.1074/jbc.273.9.4835;
RA Miech C., Dierks T., Selmer T., von Figura K., Schmidt B.;
RT "Arylsulfatase from Klebsiella pneumoniae carries a formylglycine generated
RT from a serine.";
RL J. Biol. Chem. 273:4835-4837(1998).
RN [3]
RP OXOALANINE AT SER-72.
RX PubMed=9748219; DOI=10.1074/jbc.273.40.25560;
RA Dierks T., Miech C., Hummerjohann J., Schmidt B., Kertesz M.A.,
RA von Figura K.;
RT "Posttranslational formation of formylglycine in prokaryotic sulfatases by
RT modification of either cysteine or serine.";
RL J. Biol. Chem. 273:25560-25564(1998).
CC -!- FUNCTION: Plays an important role in the mineralization of sulfates.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aryl sulfate + H2O = a phenol + H(+) + sulfate;
CC Xref=Rhea:RHEA:17261, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16189, ChEBI:CHEBI:33853, ChEBI:CHEBI:140317; EC=3.1.6.1;
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P51691};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P51691};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10336424}.
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:0000269|PubMed:9478923, ECO:0000269|PubMed:9748219}.
CC -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
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DR EMBL; AJ131525; CAB40961.1; -; Genomic_DNA.
DR PIR; T45548; T45548.
DR RefSeq; WP_004211626.1; NZ_WMNV01000002.1.
DR AlphaFoldDB; Q9X759; -.
DR SMR; Q9X759; -.
DR BindingDB; Q9X759; -.
DR ChEMBL; CHEMBL2189123; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004065; F:arylsulfatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR024607; Sulfatase_CS.
DR InterPro; IPR000917; Sulfatase_N.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR PROSITE; PS00523; SULFATASE_1; 1.
DR PROSITE; PS00149; SULFATASE_2; 1.
PE 1: Evidence at protein level;
KW Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Periplasm;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..577
FT /note="Arylsulfatase"
FT /id="PRO_0000033448"
FT ACT_SITE 72
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:9478923,
FT ECO:0000269|PubMed:9748219"
FT ACT_SITE 134
FT /evidence="ECO:0000250|UniProtKB:P15289"
FT BINDING 34
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51691"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51691"
FT BINDING 72
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /note="via 3-oxoalanine"
FT /evidence="ECO:0000250|UniProtKB:P51691"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51691"
FT BINDING 330
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P51691"
FT MOD_RES 72
FT /note="3-oxoalanine (Ser)"
FT /evidence="ECO:0000269|PubMed:9478923,
FT ECO:0000269|PubMed:9748219"
SQ SEQUENCE 577 AA; 64156 MW; 7E897EDB2CABD18C CRC64;
MNKKAMAAAV SMILAGGAHA AQQERPNVIV IIADDMGYSD ISPFGGEIPT PNLQAMAEQG
MRMSQYYTSP MSAPARSMLL TGNSNQQAGM GGMWWYDSTI GKEGYELRLT DRVTTMAERF
KDAGYNTLMA GKWHLGFVPG ATPKERGFNH AFAFMGGGTS HFNDAIPLGT VEAFHTYYTR
DGERVSLPDD FYSSEAYARQ MNSWIKATPK EQPVFAWLAF TAPHDPLQAP DEWIKRFKGQ
YEQGYAEVYR QRIARLKALG IIHDDTPLPH LELDKEWEAL TPEQQKYTAK VMQVYAAMIA
NMDAQIGTLM ETLKQTGRDK NTLLVFLTDN GANPAQGFYY ESTPEFWKQF DNSYDNVGRK
GSFVSYGPHW ANVSNAPYAN YHKTTSAQGG INTDFMISGP GITRHGKIDA STMAVYDVAP
TLYEFAGIDP NKSLAKKPVL PMIGVSFKRY LTGEVQEPPR GNYGVELHHQ AAWVDGEWKL
RRLVPRGLTA GDAPWQLFNL HDDPLETHDV AAEHPDRVKA MSEAYEAFAK RTMVTKAQGK
MIDYVGIDSK TGRYLAVDPA TMKPVPAPQA IPVSEIH
