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-APR-2013, entry version 55.
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; Enterobacteriales;
OC Enterobacteriaceae; 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
RT formation 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 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
RT generated from a serine.";
RL J. Biol. Chem. 273:4835-4837(1998).
CC -!- FUNCTION: Plays an important role in the mineralization of
CC sulfates.
CC -!- CATALYTIC ACTIVITY: A phenol sulfate + H(2)O = a phenol + sulfate.
CC -!- COFACTOR: Binds 1 calcium ion per subunit (By similarity).
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: The conversion to 3-oxoalanine (also known as C-
CC formylglycine, FGly), of a serine or cysteine residue in
CC prokaryotes and of a cysteine residue in eukaryotes, is critical
CC for catalytic activity.
CC -!- SIMILARITY: Belongs to the sulfatase family.
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DR EMBL; AJ131525; CAB40961.1; -; Genomic_DNA.
DR PIR; T45548; T45548.
DR ProteinModelPortal; Q9X759; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004065; F:arylsulfatase activity; IEA:EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.40.720.10; -; 1.
DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
DR InterPro; IPR017850; Alkaline_phosphatase_core.
DR InterPro; IPR000917; Sulfatase.
DR InterPro; IPR024607; Sulfatase_CS.
DR Pfam; PF00884; Sulfatase; 1.
DR SUPFAM; SSF53649; Alkaline_phosphatase_core; 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;
KW Periplasm; Signal.
FT SIGNAL 1 20 Potential.
FT CHAIN 21 577 Arylsulfatase.
FT /FTId=PRO_0000033448.
FT ACT_SITE 134 134 By similarity.
FT METAL 34 34 Calcium (By similarity).
FT METAL 35 35 Calcium (By similarity).
FT METAL 72 72 Calcium; via 3-oxoalanine.
FT METAL 329 329 Calcium (By similarity).
FT METAL 330 330 Calcium (By similarity).
FT MOD_RES 72 72 3-oxoalanine (Ser).
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
//
