PFEE_PSEAE
ID PFEE_PSEAE Reviewed; 304 AA.
AC Q9I0F2;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Iron(III) enterobactin esterase {ECO:0000305};
DE EC=3.1.1.108 {ECO:0000269|PubMed:30086222};
DE Flags: Precursor;
GN Name=pfeE {ECO:0000303|PubMed:30086222};
GN OrderedLocusNames=PA2689 {ECO:0000312|EMBL:AAG06077.1};
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] {ECO:0007744|PDB:6GI0, ECO:0007744|PDB:6GI1, ECO:0007744|PDB:6GI2, ECO:0007744|PDB:6GI5}
RP X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 27-304 OF WILD-TYPE; WILD-TYPE IN
RP COMPLEX WITH INHIBITOR FERRI-CATECHOL AND MUTANT ALA-182 IN COMPLEXES WITH
RP FE-ENT AND INHIBITOR FERRI-CATECHOL, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, ACTIVE SITE, AND
RP MUTAGENESIS OF SER-182 AND HIS-283.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=30086222; DOI=10.1021/acschembio.8b00543;
RA Perraud Q., Moynie L., Gasser V., Munier M., Godet J., Hoegy F., Mely Y.,
RA Mislin G.L.A., Naismith J.H., Schalk I.J.;
RT "A key role for the periplasmic PfeE esterase in iron acquisition via the
RT siderophore enterobactin in Pseudomonas aeruginosa.";
RL ACS Chem. Biol. 13:2603-2614(2018).
CC -!- FUNCTION: Catalyzes the hydrolysis of ferric enterobactin (Fe-Ent).
CC Hydrolyzes Fe-Ent into three molecules of 2,3-dihydroxybenzoylserine
CC (DHBS) still complexed with ferric iron. Iron reduction is necessary to
CC obtain complete release of the metal from DHBS. It can hydrolyze
CC salmochelin S4 (diglucosyl-C-Ent) but is not involved in iron
CC acquisition by this siderophore. {ECO:0000269|PubMed:30086222}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-enterobactin + H(+) + 3 H2O = Fe(III)-[N-(2,3-
CC dihydroxybenzoyl)-L-serine] + 2 N-(2,3-dihydroxybenzoyl)-L-serine;
CC Xref=Rhea:RHEA:30111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28199, ChEBI:CHEBI:58154, ChEBI:CHEBI:143010;
CC EC=3.1.1.108; Evidence={ECO:0000269|PubMed:30086222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30112;
CC Evidence={ECO:0000269|PubMed:30086222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-enterobactin + H2O = Fe(III)-[N-(2,3-
CC dihydroxybenzoyl)-L-serine]3 + H(+); Xref=Rhea:RHEA:59256,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28199,
CC ChEBI:CHEBI:143011; Evidence={ECO:0000269|PubMed:30086222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59257;
CC Evidence={ECO:0000269|PubMed:30086222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]3 + H(+) + H2O =
CC Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]2 + N-(2,3-
CC dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:59260, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58154, ChEBI:CHEBI:143011,
CC ChEBI:CHEBI:143012; Evidence={ECO:0000269|PubMed:30086222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59261;
CC Evidence={ECO:0000269|PubMed:30086222};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine]2 + H(+) + H2O =
CC Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] + N-(2,3-
CC dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:59264, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58154, ChEBI:CHEBI:143010,
CC ChEBI:CHEBI:143012; Evidence={ECO:0000269|PubMed:30086222};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59265;
CC Evidence={ECO:0000269|PubMed:30086222};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:30086222}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:30086222}.
CC -!- INDUCTION: Expression is induced by the presence of enterobactin in
CC bacterial environment. {ECO:0000269|PubMed:30086222}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene strongly inhibits Fe uptake
CC via enterobactin. {ECO:0000269|PubMed:30086222}.
CC -!- SIMILARITY: Belongs to the esterase D family. {ECO:0000305}.
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DR EMBL; AE004091; AAG06077.1; -; Genomic_DNA.
DR PIR; A83309; A83309.
DR RefSeq; NP_251379.1; NC_002516.2.
DR RefSeq; WP_003090549.1; NZ_QZGE01000008.1.
DR PDB; 6GI0; X-ray; 2.00 A; A/B=27-304.
DR PDB; 6GI1; X-ray; 1.66 A; A/B=27-304.
DR PDB; 6GI2; X-ray; 1.49 A; A/B=27-304.
DR PDB; 6GI5; X-ray; 3.11 A; A/B=27-304.
DR PDBsum; 6GI0; -.
DR PDBsum; 6GI1; -.
DR PDBsum; 6GI2; -.
DR PDBsum; 6GI5; -.
DR AlphaFoldDB; Q9I0F2; -.
DR SMR; Q9I0F2; -.
DR STRING; 287.DR97_5270; -.
DR ESTHER; pseae-PA2689; A85-IroE-IroD-Fes-Yiel.
DR PaxDb; Q9I0F2; -.
DR EnsemblBacteria; AAG06077; AAG06077; PA2689.
DR GeneID; 882785; -.
DR KEGG; pae:PA2689; -.
DR PATRIC; fig|208964.12.peg.2814; -.
DR PseudoCAP; PA2689; -.
DR HOGENOM; CLU_039834_3_2_6; -.
DR InParanoid; Q9I0F2; -.
DR OMA; KPWVEAN; -.
DR PhylomeDB; Q9I0F2; -.
DR BioCyc; MetaCyc:MON-20655; -.
DR BioCyc; PAER208964:G1FZ6-2729-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IDA:PseudoCAP.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000801; Esterase-like.
DR Pfam; PF00756; Esterase; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Periplasm; Reference proteome; Serine esterase;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..304
FT /note="Iron(III) enterobactin esterase"
FT /id="PRO_5004331244"
FT ACT_SITE 182
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:30086222"
FT ACT_SITE 242
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:30086222"
FT ACT_SITE 283
FT /note="Charge relay system"
FT /evidence="ECO:0000305|PubMed:30086222"
FT MUTAGEN 182
FT /note="S->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30086222"
FT MUTAGEN 283
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30086222"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 42..53
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 60..70
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 77..84
FT /evidence="ECO:0007829|PDB:6GI2"
FT HELIX 85..90
FT /evidence="ECO:0007829|PDB:6GI2"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 107..113
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 116..118
FT /evidence="ECO:0007829|PDB:6GI0"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:6GI2"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:6GI2"
FT HELIX 150..159
FT /evidence="ECO:0007829|PDB:6GI2"
FT HELIX 161..168
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 171..181
FT /evidence="ECO:0007829|PDB:6GI2"
FT HELIX 183..194
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:6GI2"
FT TURN 209..214
FT /evidence="ECO:0007829|PDB:6GI2"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:6GI2"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:6GI2"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:6GI2"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:6GI0"
FT HELIX 256..265
FT /evidence="ECO:0007829|PDB:6GI2"
FT STRAND 271..278
FT /evidence="ECO:0007829|PDB:6GI2"
FT TURN 283..285
FT /evidence="ECO:0007829|PDB:6GI2"
FT HELIX 286..296
FT /evidence="ECO:0007829|PDB:6GI2"
SQ SEQUENCE 304 AA; 32665 MW; 975AF57D2A01E4A2 CRC64;
MRTSLLVAAL GLALAAALPG GAPLAQPDPE ATMDRSLLQR QDLPYRFSAV DLDSVDGQRH
YRLWLGRPLQ APPAAGYPVV WMLDGNAAVG ALDESTLRRL ADGDAPLLVA IGYRTPLRID
RAGRTFDYTP ASPGQADQRD PLNGLPSGGA DAFLDLLRDG MRPAVAAQAP LDTARQTLWG
HSYGGLLVLH ALFTRPGEFA RYAAASPSLW WRDGAILGER AGLEQRLRGK RAELLLWRGS
AEPASPRGSL KAEPGQAMAR LVDDLRRVAG LTLDFQPLDG LGHGETLGAS LRLLLARPAV
ERQR
