LPAKS_PSEAE
ID LPAKS_PSEAE Reviewed; 658 AA.
AC Q9I5I9;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Linear primary-alkylsulfatase {ECO:0000305};
DE EC=3.1.6.21 {ECO:0000269|PubMed:16684886, ECO:0000269|PubMed:23061549};
DE AltName: Full=Sodium dodecyl sulfate hydrolase {ECO:0000303|Ref.5};
DE Short=SDS hydrolase {ECO:0000303|PubMed:16684886};
DE AltName: Full=Type III linear primary-alkylsulfatase {ECO:0000305};
DE Flags: Precursor;
GN Name=sdsA1 {ECO:0000303|PubMed:16684886};
GN OrderedLocusNames=PA0740 {ECO:0000312|EMBL:AAG04129.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=23061549; DOI=10.1111/febs.12027;
RA Knaus T., Schober M., Kepplinger B., Faccinelli M., Pitzer J., Faber K.,
RA Macheroux P., Wagner U.;
RT "Structure and mechanism of an inverting alkylsulfatase from Pseudomonas
RT sp. DSM6611 specific for secondary alkyl sulfates.";
RL FEBS J. 279:4374-4384(2012).
RN [3]
RP FUNCTION IN VIRULENCE, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=31907968; DOI=10.1111/1348-0421.12772;
RA Kida Y., Yamamoto T., Kuwano K.;
RT "SdsA1, a secreted sulfatase, contributes to the in vivo virulence of
RT Pseudomonas aeruginosa in mice.";
RL Microbiol. Immunol. 64:280-295(2020).
RN [4] {ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ, ECO:0007744|PDB:2CG2, ECO:0007744|PDB:2CG3}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC; SUBSTRATE
RP ANALOG AND SULFATE ESTER CLEAVAGE PRODUCTS, FUNCTION, CATALYTIC ACTIVITY,
RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION,
RP DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16684886; DOI=10.1073/pnas.0510501103;
RA Hagelueken G., Adams T.M., Wiehlmann L., Widow U., Kolmar H., Tuemmler B.,
RA Heinz D.W., Schubert W.D.;
RT "The crystal structure of SdsA1, an alkylsulfatase from Pseudomonas
RT aeruginosa, defines a third class of sulfatases.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7631-7636(2006).
RN [5] {ECO:0007744|PDB:5A23, ECO:0007744|PDB:5AIJ, ECO:0007744|PDB:5AJL}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, AND
RP SUBUNIT.
RX DOI=10.1107/S1600576715016556;
RA De La Mora E., Flores-Hernandez E., Jakoncic J., Stojanoff V., Siliqi D.,
RA Sanchez-Puig N., Moreno A.;
RT "Sdsa polymorph isolation and improvement of their crystal quality using
RT nonconventional crystallization techniques.";
RL J. Appl. Crystallogr. 48:1551-1551(2015).
CC -!- FUNCTION: Alkylsulfatase that cleaves both short and medium-length
CC alkylsulfates, including the widely used detergent sodium dodecyl
CC sulfate (SDS) (PubMed:16684886). Acts in vitro on primary alkylsulfates
CC such as decyl sulfate, octyl sulfate and hexyl sulfate, but not on
CC sulfated sugars and arylsulfates (PubMed:16684886, PubMed:23061549).
CC The hydrolysis of SDS allows the bacterium to use SDS as a sole carbon
CC or sulfur source (PubMed:16684886). In addition, contributes to the in
CC vivo virulence of P.aeruginosa by playing a central role in the
CC degradation of mucin, a glycoprotein that is the primary component of
CC the mucus overlaying the host epithelial tissues (PubMed:31907968).
CC Plays a role in the degradation of both protein and carbohydrate
CC moieties in mucin via the release of sulfate from mucin, D-galactose 6-
CC sulfate (Gal-6S) and N-acetyl-D-glucosamine 6-sulfate (GlcNAc-6S)
CC (PubMed:31907968). {ECO:0000269|PubMed:16684886,
CC ECO:0000269|PubMed:23061549, ECO:0000269|PubMed:31907968}.
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:0000269|PubMed:16684886, ECO:0000269|PubMed:23061549};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67909;
CC Evidence={ECO:0000269|PubMed:16684886};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:16684886,
CC ECO:0000269|Ref.5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9 uM for SDS {ECO:0000269|PubMed:16684886};
CC KM=30 uM for 1-octyl sulfate {ECO:0000269|PubMed:23061549};
CC KM=605 uM for (R)-2-octyl sulfate {ECO:0000269|PubMed:23061549};
CC Note=kcat is 337 min(-1) with 1-octyl sulfate as substrate. kcat is
CC 5.4 min(-1) with (R)-2-octyl sulfate as substrate.
CC {ECO:0000269|PubMed:23061549};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5}.
CC -!- INTERACTION:
CC Q9I5I9; Q9I5I9: sdsA1; NbExp=7; IntAct=EBI-11666189, EBI-11666189;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:16684886}.
CC -!- INDUCTION: Up-regulated in mucin minimal medium.
CC {ECO:0000269|PubMed:31907968}.
CC -!- DOMAIN: Contains three distinct domains: an N-terminal catalytic domain
CC that contains a binuclear Zn(2+) cluster, a central dimerization domain
CC that ensures resistance to high concentrations of SDS and a C-terminal
CC domain that provides a hydrophobic groove, presumably to recruit long
CC aliphatic substrates (PubMed:16684886). Although separated by the
CC dimerization domain in terms of sequence, the N-terminal and C-terminal
CC domains are spatially directly adjacent (PubMed:16684886).
CC {ECO:0000269|PubMed:16684886}.
CC -!- DISRUPTION PHENOTYPE: Insertion mutant cannot grow with SDS as a sole
CC carbon and/or sulfur source (PubMed:16684886). Disruption of the gene
CC leads to a decrease in the growth in mucin minimal medium and a
CC reduction in the degradation of both carbohydrate and protein moieties
CC in mucin (PubMed:31907968). Mutant shows reduced swimming, swarming and
CC twitching motilities and decreased mucin gel penetration ability
CC (PubMed:31907968). Virulence of the mutant is attenuated in leukopenic
CC mice compared with the wild-type strain (PubMed:31907968).
CC {ECO:0000269|PubMed:16684886, ECO:0000269|PubMed:31907968}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC sulfatase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG04129.1; -; Genomic_DNA.
DR PIR; G83552; G83552.
DR RefSeq; NP_249431.1; NC_002516.2.
DR RefSeq; WP_003114166.1; NZ_QZGE01000007.1.
DR PDB; 2CFU; X-ray; 1.90 A; A=1-658.
DR PDB; 2CFZ; X-ray; 2.05 A; A=1-658.
DR PDB; 2CG2; X-ray; 2.10 A; A=1-658.
DR PDB; 2CG3; X-ray; 2.60 A; A=1-658.
DR PDB; 5A23; X-ray; 2.41 A; A/B/C/D=1-658.
DR PDB; 5AIJ; X-ray; 1.95 A; A=1-658.
DR PDB; 5AJL; X-ray; 3.45 A; A/B=1-658.
DR PDBsum; 2CFU; -.
DR PDBsum; 2CFZ; -.
DR PDBsum; 2CG2; -.
DR PDBsum; 2CG3; -.
DR PDBsum; 5A23; -.
DR PDBsum; 5AIJ; -.
DR PDBsum; 5AJL; -.
DR AlphaFoldDB; Q9I5I9; -.
DR SASBDB; Q9I5I9; -.
DR SMR; Q9I5I9; -.
DR DIP; DIP-61164N; -.
DR MINT; Q9I5I9; -.
DR STRING; 287.DR97_1244; -.
DR DrugBank; DB06894; 1-Dodecanol.
DR DrugBank; DB06893; Decylsulfonic acid.
DR PaxDb; Q9I5I9; -.
DR PRIDE; Q9I5I9; -.
DR EnsemblBacteria; AAG04129; AAG04129; PA0740.
DR GeneID; 882069; -.
DR KEGG; pae:PA0740; -.
DR PATRIC; fig|208964.12.peg.769; -.
DR PseudoCAP; PA0740; -.
DR HOGENOM; CLU_014655_1_0_6; -.
DR InParanoid; Q9I5I9; -.
DR OMA; KWETLTI; -.
DR PhylomeDB; Q9I5I9; -.
DR BioCyc; PAER208964:G1FZ6-753-MON; -.
DR BRENDA; 3.1.6.21; 5087.
DR EvolutionaryTrace; Q9I5I9; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0018741; F:alkyl sulfatase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Periplasm; Reference proteome;
KW Signal; Virulence; Zinc.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..658
FT /note="Linear primary-alkylsulfatase"
FT /id="PRO_5004328509"
FT BINDING 169
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ,
FT ECO:0007744|PDB:2CG2, ECO:0007744|PDB:2CG3,
FT ECO:0007744|PDB:5A23, ECO:0007744|PDB:5AIJ,
FT ECO:0007744|PDB:5AJL"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ,
FT ECO:0007744|PDB:2CG2, ECO:0007744|PDB:2CG3,
FT ECO:0007744|PDB:5A23, ECO:0007744|PDB:5AIJ,
FT ECO:0007744|PDB:5AJL"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ,
FT ECO:0007744|PDB:2CG2, ECO:0007744|PDB:2CG3,
FT ECO:0007744|PDB:5A23, ECO:0007744|PDB:5AIJ,
FT ECO:0007744|PDB:5AJL"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ,
FT ECO:0007744|PDB:2CG2, ECO:0007744|PDB:2CG3,
FT ECO:0007744|PDB:5A23, ECO:0007744|PDB:5AIJ,
FT ECO:0007744|PDB:5AJL"
FT BINDING 280
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ,
FT ECO:0007744|PDB:2CG2, ECO:0007744|PDB:5A23,
FT ECO:0007744|PDB:5AIJ, ECO:0007744|PDB:5AJL"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ,
FT ECO:0007744|PDB:2CG2, ECO:0007744|PDB:5A23,
FT ECO:0007744|PDB:5AIJ, ECO:0007744|PDB:5AJL"
FT BINDING 299
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ,
FT ECO:0007744|PDB:2CG2, ECO:0007744|PDB:2CG3,
FT ECO:0007744|PDB:5A23, ECO:0007744|PDB:5AIJ,
FT ECO:0007744|PDB:5AJL"
FT BINDING 307..312
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000269|PubMed:16684886,
FT ECO:0007744|PDB:2CG2"
FT BINDING 317
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000269|PubMed:16684886,
FT ECO:0007744|PDB:2CG2"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16684886, ECO:0000269|Ref.5,
FT ECO:0007744|PDB:2CFU, ECO:0007744|PDB:2CFZ,
FT ECO:0007744|PDB:2CG2, ECO:0007744|PDB:2CG3,
FT ECO:0007744|PDB:5A23, ECO:0007744|PDB:5AIJ,
FT ECO:0007744|PDB:5AJL"
FT BINDING 405
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000269|PubMed:16684886,
FT ECO:0007744|PDB:2CG2"
SQ SEQUENCE 658 AA; 72592 MW; 3D29B5D2B0A2A84F CRC64;
MSRLLALLAL APLLAGAAET TAPKPPSAFT VEAQRRVEAE LPFADRADFE RADRGLIRRP
ERLLIRNPDG SVAWQLGGYD FLLDGKPRDS INPSLQRQAL LNLKYGLFEV AEGIYQVRGF
DLANITFIRG DSGWIVVDTL TTPATARAAY ELVSRELGER PIRTVIYSHA HADHFGGVRG
LVEPQQVASG AVQIIAPAGF MEAAIKENVL AGNAMMRRAT YQYGTQLPKG PQGQVDMAIG
KGLARGPLSL LAPTRLIEGE GEDLVLDGVP FTFQNTPGTE SPAEMNIWLP RQKALLMAEN
VVGTLHNLYT LRGAEVRDAL GWSKYINQAL HRFGRQAEVM FAVHNWPRWG NAEIVEVLEK
QRDLYGYLHD QTLHLANQGV TIGQVHNRLR LPPSLDQEWY DRGYHGSVSH NARAVLNRYL
GYYDGNPATL DPLSPEDSAG RYVEYMGGAE RLLEQARASY ARGEYRWVVE VVNRLVFAEP
DNRAARELQA DALEQLGYQA ENAGWRNSYL SAAYELRHGV PRDQPTMKAG SADALAAMDT
GLLFDYLGVR LDAGAAEGKA LSINLRLPDI GENYLLELKN SHLNNLRGVQ SEDAGQTVSI
DRADLNRLLL KEVSAVRLVF EGKLKSSGNP LLLGQLFGML GDFDFWFDIV TPAAKSEG
