ID   ASLA_ECOLI              Reviewed;         551 AA.
AC   P25549; Q2M8A6;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=Putative sulfatase AslA;
DE            EC=3.1.6.-;
DE   Flags: Precursor;
GN   Name=aslA {ECO:0000303|Ref.1}; Synonyms=atsA {ECO:0000303|PubMed:361719};
GN   OrderedLocusNames=b3801, JW3773;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RA   Murphy H.R., Kalman M., Cashel M.;
RT   "Identification of the gppB locus as two convergent arylsulfatase-like
RT   genes, aslA and aslB, capable of suppressing a guanosine pentaphosphate
RT   phosphatase missense mutation in Escherichia coli.";
RL   Submitted (APR-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=1379743; DOI=10.1126/science.1379743;
RA   Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT   84.5 to 86.5 minutes.";
RL   Science 257:771-778(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NOT ARYLSULFATASE.
RC   STRAIN=B, C, K12,
RC   K12 / C600 / CR34 / ATCC 23724 / DSM 3925 / LMG 3041 / NCIB 10222, and
RC   K12 / W3350 / ATCC 27020;
RX   PubMed=361719; DOI=10.1128/jb.136.2.714-722.1978;
RA   Murooka Y., Higashiura T., Harada T.;
RT   "Genetic mapping of tyramine oxidase and arylsulfatase genes and their
RT   regulation in intergeneric hybrids of enteric bacteria.";
RL   J. Bacteriol. 136:714-722(1978).
CC   -!- FUNCTION: No E.coli strains have been observed to have an arylsulfatase
CC       activity. A 'latent' activity has been observed by heterologous
CC       expression of a genomic region linked to tynA, but it does not map near
CC       aslA. {ECO:0000269|PubMed:361719}.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000250|UniProtKB:P15289};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250,
CC       ECO:0000250|UniProtKB:P15289};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
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:0000250|UniProtKB:P15289}.
CC   -!- SIMILARITY: Belongs to the sulfatase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC32036.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; M90498; AAC32036.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; M87049; AAA67597.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76804.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77500.1; -; Genomic_DNA.
DR   PIR; S30691; S30691.
DR   RefSeq; NP_418245.1; NC_000913.3.
DR   RefSeq; WP_000395863.1; NZ_SSZK01000025.1.
DR   AlphaFoldDB; P25549; -.
DR   SMR; P25549; -.
DR   BioGRID; 4262605; 5.
DR   IntAct; P25549; 1.
DR   STRING; 511145.b3801; -.
DR   PaxDb; P25549; -.
DR   PRIDE; P25549; -.
DR   EnsemblBacteria; AAC76804; AAC76804; b3801.
DR   EnsemblBacteria; BAE77500; BAE77500; BAE77500.
DR   GeneID; 949015; -.
DR   KEGG; ecj:JW3773; -.
DR   KEGG; eco:b3801; -.
DR   PATRIC; fig|1411691.4.peg.2908; -.
DR   EchoBASE; EB0087; -.
DR   eggNOG; COG3119; Bacteria.
DR   HOGENOM; CLU_006332_10_0_6; -.
DR   InParanoid; P25549; -.
DR   OMA; PALEPCC; -.
DR   PhylomeDB; P25549; -.
DR   BioCyc; EcoCyc:ARYLSULFAT-MON; -.
DR   BioCyc; MetaCyc:ARYLSULFAT-MON; -.
DR   PRO; PR:P25549; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004065; F:arylsulfatase activity; IBA:GO_Central.
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   3: Inferred from homology;
KW   Calcium; Hydrolase; Metal-binding; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..551
FT                   /note="Putative sulfatase AslA"
FT                   /id="PRO_0000033446"
FT   ACT_SITE        136
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         94
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         95
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         136
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /note="via 3-oxoalanine"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         356
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   BINDING         357
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   MOD_RES         136
FT                   /note="3-oxoalanine (Ser)"
FT                   /evidence="ECO:0000250|UniProtKB:P15289"
FT   CONFLICT        191
FT                   /note="M -> I (in Ref. 1; AAC32036)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  60718 MW;  A04C8BBE5E63E988 CRC64;
     MEFSFSPKRL VVAVAAALPL MASAADTPST ATARKGFAGY DHPNQYLVKP ATTIADNMMP
     VMQHPAQDKE TQQKLAELEK KTGKKPNVVV FLLDDVGWMD VGFNGGGVAV GNPTPDIDAV
     ASQGLILTSA YSQPSSSPTR ATILTGQYSI HHGILMPPMY GQPGGLQGLT TLPQLLHDQG
     YVTQAIGKWH MGENKESQPQ NVGFDDFRGF NSVSDMYTEW RDVHVNPEVA LSPDRSEYIK
     QLPFSKDDVH AVRGGEQQAI ADITPKYMED LDQRWMDYGV KFLDKMAKSD KPFFLYYGTR
     GCHFDNYPNA KYAGSSPART SYGDCMVEMN DVFANLYKTL EKNGQLDNTL IVFTSDNGPE
     AEVPPHGRTP FRGAKGSTWE GGVRVPTFVY WKGMIQPRKS DGIVDLADLF PTALDLAGHP
     GAKVANLVPK TTFIDGVDQT SFFLGTNGQS NRKAEHYFLN GKLAAVRMDE FKYHVLIQQP
     YAYTQSGYQG GFTGTVMQTA GSSVFNLYTD PQESDSIGVR HIPMGVPLQT EMHAYMEILK
     KYPPRAQIKS D