LPAKS_PSES9
ID LPAKS_PSES9 Reviewed; 528 AA.
AC Q52556;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Linear primary-alkylsulfatase {ECO:0000250|UniProtKB:Q9I5I9};
DE EC=3.1.6.21 {ECO:0000250|UniProtKB:Q9I5I9};
DE AltName: Full=SDSase {ECO:0000303|PubMed:1587481};
DE AltName: Full=Type III linear primary-alkylsulfatase {ECO:0000250|UniProtKB:Q9I5I9};
GN Name=sdsA {ECO:0000303|PubMed:1587481};
OS Pseudomonas sp. (strain ATCC 19151).
OC Bacteria; Proteobacteria.
OX NCBI_TaxID=315;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 19151;
RX PubMed=1587481; DOI=10.1016/0378-1119(92)90702-q;
RA Davison J., Brunel F., Phanopoulos A., Prozzi D., Terpstra P.;
RT "Cloning and sequencing of Pseudomonas genes determining sodium dodecyl
RT sulfate biodegradation.";
RL Gene 114:19-24(1992).
CC -!- FUNCTION: Alkylsulfatase that cleaves the widely used detergent sodium
CC dodecyl sulfate (SDS), which allows the bacterium to use SDS as a sole
CC carbon or sulfur source. {ECO:0000305|PubMed:1587481}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary linear alkyl sulfate ester + H2O = a primary alcohol
CC + H(+) + sulfate; Xref=Rhea:RHEA:67908, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:16189,
CC ChEBI:CHEBI:157685; EC=3.1.6.21;
CC Evidence={ECO:0000250|UniProtKB:Q9I5I9};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:Q9I5I9};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9I5I9};
CC -!- INDUCTION: Transcriptionally regulated by SdsB.
CC {ECO:0000269|PubMed:1587481}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC sulfatase family. {ECO:0000305}.
CC -!- CAUTION: The N-terminus is shorter than orthologs. {ECO:0000305}.
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DR EMBL; M86744; AAA25989.1; -; Genomic_DNA.
DR PIR; JC1118; JC1118.
DR GO; GO:0018741; F:alkyl sulfatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0018909; P:dodecyl sulfate metabolic process; IEA:InterPro.
DR CDD; cd07710; arylsulfatase_Sdsa1-like_MBL-fold; 1.
DR Gene3D; 1.25.40.880; -; 1.
DR Gene3D; 3.30.1050.10; -; 1.
DR InterPro; IPR038536; Alkyl/aryl-sulf_dimr_sf.
DR InterPro; IPR029229; Alkyl_sulf_C.
DR InterPro; IPR029228; Alkyl_sulf_dimr.
DR InterPro; IPR044097; Bds1/SdsA1_MBL-fold.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR InterPro; IPR036527; SCP2_sterol-bd_dom_sf.
DR Pfam; PF14864; Alkyl_sulf_C; 1.
DR Pfam; PF14863; Alkyl_sulf_dimr; 1.
DR Pfam; PF00753; Lactamase_B; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF55718; SSF55718; 1.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 2: Evidence at transcript level;
KW Hydrolase; Metal-binding; Zinc.
FT CHAIN 1..528
FT /note="Linear primary-alkylsulfatase"
FT /id="PRO_0000455160"
FT BINDING 42
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 44
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 46
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 47
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 170
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 179..184
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000250|UniProtKB:P32717"
FT BINDING 189
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000250|UniProtKB:P32717"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 275
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000250|UniProtKB:P32717"
SQ SEQUENCE 528 AA; 58950 MW; 50539398C2541BBB CRC64;
MIEAPEGLII VDTGESVDQS RKVLAEFRKI SDKPIKAIVY THFHPDHING VKAFVSEEQV
KSGEVRIYAQ ETLLDNVVTQ GSLVGPILTM RSGYSFGVAL SDEDKRDMNA GLGPLAHEGA
STFIAPTDTF RDSLDTTIAG LKVQFLHVPS EAPDEIVLYL PDNRVLISAE VTQGPTLPNV
HTLRGTKFRD PVVWVASLDK LRAFQADVMV PLHGQPVSGR EKVEEVLRMT RDAIAYIHDQ
TVRWMNKGLT PDELVEKVKL PPHLAGYTPY LREYYGTVKH SVRQIYQGYL GWFQGDPVDL
DPIPPAEKAR RLIALMGGRD KVLMAAGDAY LKGDWQWAAE LSGYAIRVDH DDKLARDIKA
RSFRRLGYAS MNINWRNWYL MSAMELEGKL EGDVALEMSR RVRAAFLSPD MLKNLPARIF
LQNWVTRIDP EKSGDVELAL GFAFPDIDEA WTLEVRRGVA QLKSGIDPAV PLRLTLDKRY
LDTVISGENS LLKGALLGDV KVDGNLLDIK TFLGCFDFED APIALTVR
