LPAKS_ECOLI
ID LPAKS_ECOLI Reviewed; 661 AA.
AC P32717; Q2M6M1;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Linear primary-alkylsulfatase {ECO:0000305};
DE EC=3.1.6.21 {ECO:0000269|PubMed:25066955};
DE AltName: Full=Type III linear primary-alkylsulfatase {ECO:0000305};
DE Flags: Precursor;
GN Name=yjcS; OrderedLocusNames=b4083, JW5721;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 614.
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 [3]
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 [4] {ECO:0007744|PDB:4PDX}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 30-661 IN COMPLEX WITH SULFATE,
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, OVEREXPRESSION, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, AND
RP MUTAGENESIS OF 184-ASP-HIS-185.
RX PubMed=25066955; DOI=10.1002/pro.2528;
RA Liang Y., Gao Z., Dong Y., Liu Q.;
RT "Structural and functional analysis show that the Escherichia coli
RT uncharacterized protein YjcS is likely an alkylsulfatase.";
RL Protein Sci. 23:1442-1450(2014).
CC -!- FUNCTION: Alkylsulfatase that cleaves the widely used detergent sodium
CC dodecyl sulfate (SDS). {ECO:0000269|PubMed:25066955}.
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:25066955};
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 -!- ACTIVITY REGULATION: In vitro, is slightly activated in the presence of
CC Ca(2+), but inhibited by Zn(2+). {ECO:0000269|PubMed:25066955}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:25066955}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:25066955}.
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 domain
CC (PubMed:25066955). Although separated by the dimerization domain in
CC terms of sequence, the N-terminal and C-terminal domains are spatially
CC directly adjacent (PubMed:25066955). {ECO:0000269|PubMed:25066955}.
CC -!- MISCELLANEOUS: E.coli BL21 cells were shown to not grow on minimal
CC medium agarose plates containing 0.1% SDS, indicating that the SDS was
CC toxic to the bacteria cells. However, overexpression of YjcS in these
CC cells rescued the cells. {ECO:0000269|PubMed:25066955}.
CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. Type III
CC sulfatase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC43177.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00006; AAC43177.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77044.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78085.1; -; Genomic_DNA.
DR PIR; B65217; B65217.
DR RefSeq; NP_418507.2; NC_000913.3.
DR RefSeq; WP_001066019.1; NZ_SSZK01000016.1.
DR PDB; 4PDX; X-ray; 1.75 A; A/B=30-661.
DR PDBsum; 4PDX; -.
DR AlphaFoldDB; P32717; -.
DR SMR; P32717; -.
DR BioGRID; 4262954; 7.
DR STRING; 511145.b4083; -.
DR jPOST; P32717; -.
DR PaxDb; P32717; -.
DR PRIDE; P32717; -.
DR EnsemblBacteria; AAC77044; AAC77044; b4083.
DR EnsemblBacteria; BAE78085; BAE78085; BAE78085.
DR GeneID; 948597; -.
DR KEGG; ecj:JW5721; -.
DR KEGG; eco:b4083; -.
DR PATRIC; fig|511145.12.peg.4209; -.
DR EchoBASE; EB1898; -.
DR eggNOG; COG2015; Bacteria.
DR HOGENOM; CLU_014655_1_0_6; -.
DR InParanoid; P32717; -.
DR OMA; NPARLWP; -.
DR PhylomeDB; P32717; -.
DR BioCyc; EcoCyc:EG11955-MON; -.
DR BioCyc; MetaCyc:EG11955-MON; -.
DR BRENDA; 3.1.6.21; 2026.
DR PRO; PR:P32717; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0018741; F:alkyl sulfatase activity; IDA:EcoCyc.
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; IMP:EcoCyc.
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; Zinc.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:25066955"
FT CHAIN 30..661
FT /note="Linear primary-alkylsulfatase"
FT /id="PRO_0000169726"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 182
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 291
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 310
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 318..323
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000269|PubMed:25066955,
FT ECO:0007744|PDB:4PDX"
FT BINDING 328
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000269|PubMed:25066955,
FT ECO:0007744|PDB:4PDX"
FT BINDING 355
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q9I5I9"
FT BINDING 416
FT /ligand="sulfate"
FT /ligand_id="ChEBI:CHEBI:16189"
FT /evidence="ECO:0000269|PubMed:25066955,
FT ECO:0007744|PDB:4PDX"
FT MUTAGEN 184..185
FT /note="DH->NA: Loss of activity."
FT /evidence="ECO:0000269|PubMed:25066955"
FT CONFLICT 614
FT /note="H -> D (in Ref. 1; AAC43177)"
FT /evidence="ECO:0000305"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 79..81
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 87..90
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 104..113
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 117..122
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 125..134
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 142..148
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:4PDX"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4PDX"
FT TURN 186..188
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 195..199
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:4PDX"
FT TURN 218..222
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 223..233
FT /evidence="ECO:0007829|PDB:4PDX"
FT TURN 234..237
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 280..286
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 330..344
FT /evidence="ECO:0007829|PDB:4PDX"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 350..352
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 362..388
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 404..407
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 419..431
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 438..440
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 446..456
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 460..472
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 476..489
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 494..510
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 514..529
FT /evidence="ECO:0007829|PDB:4PDX"
FT TURN 544..547
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 550..560
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 563..566
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 570..576
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 582..588
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 591..597
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 603..607
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 610..617
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 623..628
FT /evidence="ECO:0007829|PDB:4PDX"
FT TURN 629..631
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 633..636
FT /evidence="ECO:0007829|PDB:4PDX"
FT HELIX 640..645
FT /evidence="ECO:0007829|PDB:4PDX"
FT STRAND 657..659
FT /evidence="ECO:0007829|PDB:4PDX"
SQ SEQUENCE 661 AA; 73151 MW; 64D5037ACEF5E455 CRC64;
MNNSRLFRLS RIVIALTAAS GMMVNTANAK EEAKAATQYT QQVNQNYAKS LPFSDRQDFD
DAQRGFIAPL LDEGILRDAN GKVYYRADDY KFDINAAAPE TVNPSLWRQS QINGISGLFK
VTDKMYQVRG QDISNITFVE GEKGIIVIDP LVTPPAAKAA LDLYFQHRPQ KPIVAVIYTH
SHTDHYGGVK GIISEADVKS GKVQVIAPAG FMDEAISENV LAGNIMSRRA LYSYGLLLPH
NAQGNVGNGL GVTLATGDPS IIAPTKTIVR TGEKMIIDGL EFDFLMTPGS EAPAEMHFYI
PALKALCTAE NATHTLHNFY TLRGAKTRDT SKWTEYLNET LDMWGNDAEV LFMPHTWPVW
GNKHINDYIG KYRDTIKYIH DQTLHLANQG YTMNEIGDMI KLPPALANNW ASRGYYGSVS
HNARAVYNFY LGYYDGNPAN LHPYGQVEMG KRYVQALGGS ARVINLAQEA NKQGDYRWSA
ELLKQVIAAN PGDQVAKNLQ ANNFEQLGYQ AESATWRGFY LTGAKELREG VHKFSHGTTG
SPDTIRGMSV EMLFDFMAVR LDSAKAAGKN ISLNFNMSNG DNLNLTLNDS VLNYRKTLQP
QADASFYISR EDLHAVLTGQ AKMADLVKAK KAKIIGNGAK LEEIIACLDN FDLWVNIVTP
N
