LPAKS_PSESP
ID LPAKS_PSESP Reviewed; 674 AA.
AC F2WP51;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 31-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 40.
DE RecName: Full=Linear primary-alkylsulfatase {ECO:0000305};
DE EC=3.1.6.21 {ECO:0000269|PubMed:21318560, ECO:0000269|PubMed:28442601};
DE AltName: Full=Primary type-III alkylsulfatase {ECO:0000303|PubMed:28442601};
DE AltName: Full=Type III linear primary-alkylsulfatase {ECO:0000305};
DE Flags: Precursor;
GN Name=sdsAP {ECO:0000303|PubMed:21318560};
GN Synonyms=psdsA {ECO:0000312|EMBL:AEA06493.1};
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND
RP BIOTECHNOLOGY.
RC STRAIN=S9;
RX PubMed=21318560; DOI=10.1007/s00792-011-0357-4;
RA Long M., Ruan L., Li F., Yu Z., Xu X.;
RT "Heterologous expression and characterization of a recombinant thermostable
RT alkylsulfatase (sdsAP).";
RL Extremophiles 15:293-301(2011).
RN [2] {ECO:0007744|PDB:4NUR}
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) OF 42-674 IN COMPLEX WITH ZINC,
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF TYR-246 AND GLY-263.
RC STRAIN=S9;
RX PubMed=28442601; DOI=10.1042/bsr20170001;
RA Sun L., Chen P., Su Y., Cai Z., Ruan L., Xu X., Wu Y.;
RT "Crystal structure of thermostable alkylsulfatase SdsAP from Pseudomonas
RT sp. S9.";
RL Biosci. Rep. 37:0-0(2017).
CC -!- FUNCTION: Alkylsulfatase that cleaves primary alkyl sulfates such as
CC sodium octyl sulfate and the widely used detergent sodium dodecyl
CC sulfate (SDS). {ECO:0000269|PubMed:21318560,
CC ECO:0000269|PubMed:28442601}.
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:21318560, ECO:0000269|PubMed:28442601};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:21318560, ECO:0000269|PubMed:28442601};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q9I5I9};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. Slightly activated in the
CC presence of Ca(2+). {ECO:0000269|PubMed:21318560}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=264.3 uM for SDS {ECO:0000269|PubMed:21318560};
CC KM=74.2 uM for SDS {ECO:0000269|PubMed:28442601};
CC Vmax=33.8 umol/min/mg enzyme {ECO:0000269|PubMed:21318560};
CC Note=kcat is 4.88 sec(-1) with SDS as substrate.
CC {ECO:0000269|PubMed:28442601};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:21318560};
CC Temperature dependence:
CC Optimum temperature is 70 degrees Celsius. Retains more than 90%
CC activity after incubation at 65 degrees Celsius for 1 hour.
CC {ECO:0000269|PubMed:21318560};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21318560,
CC ECO:0000269|PubMed:28442601}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:Q9I5I9}.
CC -!- DOMAIN: Contains three distinct domains: an N-terminal catalytic domain
CC that contains a binuclear Zn(2+) cluster, a central dimerization domain
CC and a C-terminal sterol carrier protein type 2 (SCP-2)-like fold
CC domain. {ECO:0000269|PubMed:28442601}.
CC -!- BIOTECHNOLOGY: The thermal stability and higher specific activities
CC make it an ideal candidate for the application in the biodegradation of
CC SDS-containing waste water under elevated temperature conditions.
CC {ECO:0000269|PubMed:21318560}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC sulfatase family. {ECO:0000305}.
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DR EMBL; HQ189533; AEA06493.1; -; Genomic_DNA.
DR PDB; 4NUR; X-ray; 1.76 A; A/B=42-674.
DR PDBsum; 4NUR; -.
DR SMR; F2WP51; -.
DR KEGG; ag:AEA06493; -.
DR BRENDA; 3.1.6.21; 17958.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Periplasm; Signal; Zinc.
FT SIGNAL 1..41
FT /evidence="ECO:0000255"
FT CHAIN 42..674
FT /note="Linear primary-alkylsulfatase"
FT /id="PRO_5003292034"
FT BINDING 192
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 194
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28442601,
FT ECO:0007744|PDB:4NUR"
FT BINDING 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28442601,
FT ECO:0007744|PDB:4NUR"
FT BINDING 303
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28442601,
FT ECO:0007744|PDB:4NUR"
FT BINDING 330..335
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000250|UniProtKB:P32717"
FT BINDING 340
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000250|UniProtKB:P32717"
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:28442601,
FT ECO:0007744|PDB:4NUR"
FT BINDING 428
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000250|UniProtKB:P32717"
FT MUTAGEN 246
FT /note="Y->A,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28442601"
FT MUTAGEN 263
FT /note="G->A,F: Loss of activity."
FT /evidence="ECO:0000269|PubMed:28442601"
SQ SEQUENCE 674 AA; 75040 MW; 68E7909A36DC12F5 CRC64;
MKLNALSTAT HGSRSSPVKL WKFSTSFLLA ASIIVSGQSW AAETAKPATD ATKAANDALL
KELPFDDKTS FDLAHKGFIA PLPAEPIKGE KGNMIWDPSK YGFIKEGEAA PDTTNPSLWR
QSQLINISGL FEVTDGIYQV RNYDLSNMTI VEGKDGITIF DPLISQETAK AALDLYYKHR
PKKPVVAVIY THSHVDHYGG VRGVVDEADV KAGKVKIYAP LGFLEHAVAE NVMAGTAMSR
RASYMYGNLL PPDAKGQLGA GLGTTTSAGT VTLIPPTDII KETGETHVID GLTYEFMYAP
GSEAPAEMLY YIKEKKALNA AEDSTHTLHN TYSLRGAKIR DPLAWSKYLN EALKLWGDDV
QVMYAMHHWP VWGNKEVREQ LSLQRDMYRY INDETLRLAN KGYTMTEIAE QVKLPKKIAT
KFSNRGYYGS LNHNVKATYV LYLGWFIGNP ATLWELPPAD KAKRYVEMMG GADAVLKKAK
EYYDKGDFRW VAEVVNHVVF AEPNNQAAKN MQADALEQLG YQAESGPWRN FYLTGAQELR
NGVQQLPTPD TASPDTVKAM DLDLFFDFLA MRLKGPDVAD KHITLNLDFT DLKQKYTLEM
VNGVLNHTEG MQAKNADATV TLTRETLNNV MLKQTTLKDA ESSGDIKIEG DKGKLEELMS
YMDNFDFWFN IVTP
