SPUE_PSEAE
ID SPUE_PSEAE Reviewed; 365 AA.
AC Q9I6J0;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Spermidine-binding periplasmic protein SpuE;
DE Flags: Precursor;
GN Name=spuE; OrderedLocusNames=PA0301;
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 X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 28-362 OF APOPROTEIN AND IN
RP COMPLEX WITH SPERMIDINE, FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP TRP-271.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=22300763; DOI=10.1016/j.jmb.2012.01.010;
RA Wu D., Lim S.C., Dong Y., Wu J., Tao F., Zhou L., Zhang L.H., Song H.;
RT "Structural basis of substrate binding specificity revealed by the crystal
RT structures of polyamine receptors SpuD and SpuE from Pseudomonas
RT aeruginosa.";
RL J. Mol. Biol. 416:697-712(2012).
CC -!- FUNCTION: Spermidine-binding protein probably required for its uptake
CC into cells. Binds spermidine with high affinity (KD=14.3 nM). Does not
CC bind putrescine, cadaverine or spermine. Spermidine binding induces
CC large inter-domain conformational changes. Implicated in induction of
CC type 3 secretion systems (T3SS), which play a role in virulence.
CC {ECO:0000269|PubMed:22300763}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|PIRNR:PIRNR019574}.
CC -!- DISRUPTION PHENOTYPE: Significant decrease in T3SS induction.
CC {ECO:0000269|PubMed:22300763}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein PotD/PotF
CC family. {ECO:0000255|PIRNR:PIRNR019574}.
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DR EMBL; AE004091; AAG03690.1; -; Genomic_DNA.
DR PIR; F83607; F83607.
DR RefSeq; NP_248992.1; NC_002516.2.
DR RefSeq; WP_003084301.1; NZ_QZGE01000016.1.
DR PDB; 3TTL; X-ray; 2.30 A; A/B=28-362.
DR PDB; 3TTN; X-ray; 2.00 A; A/B=28-362.
DR PDB; 6IKM; X-ray; 3.40 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=28-362.
DR PDBsum; 3TTL; -.
DR PDBsum; 3TTN; -.
DR PDBsum; 6IKM; -.
DR AlphaFoldDB; Q9I6J0; -.
DR SMR; Q9I6J0; -.
DR STRING; 287.DR97_3263; -.
DR PaxDb; Q9I6J0; -.
DR PRIDE; Q9I6J0; -.
DR ABCD; Q9I6J0; 3 sequenced antibodies.
DR EnsemblBacteria; AAG03690; AAG03690; PA0301.
DR GeneID; 877626; -.
DR KEGG; pae:PA0301; -.
DR PATRIC; fig|208964.12.peg.315; -.
DR PseudoCAP; PA0301; -.
DR HOGENOM; CLU_026974_1_4_6; -.
DR InParanoid; Q9I6J0; -.
DR OMA; YANPNPK; -.
DR PhylomeDB; Q9I6J0; -.
DR BioCyc; PAER208964:G1FZ6-303-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005615; C:extracellular space; IDA:PseudoCAP.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0019809; F:spermidine binding; IDA:PseudoCAP.
DR GO; GO:0015846; P:polyamine transport; IMP:PseudoCAP.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR001188; Sperm_putr-bd.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1.
DR PRINTS; PR00909; SPERMDNBNDNG.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Reference proteome; Signal; Transport; Virulence.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..365
FT /note="Spermidine-binding periplasmic protein SpuE"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431397"
FT BINDING 35
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:22300763"
FT BINDING 181
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:22300763"
FT BINDING 242
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:22300763"
FT BINDING 269
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000269|PubMed:22300763"
FT MUTAGEN 271
FT /note="W->F: Increases affinity for putrescine (to KD=1.12
FT uM)."
FT /evidence="ECO:0000269|PubMed:22300763"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 42..50
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 62..70
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 111..117
FT /evidence="ECO:0007829|PDB:3TTN"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 126..140
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 179..189
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 199..212
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:3TTL"
FT HELIX 224..229
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 240..253
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 284..294
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 297..307
FT /evidence="ECO:0007829|PDB:3TTN"
FT STRAND 310..312
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:3TTN"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 334..337
FT /evidence="ECO:0007829|PDB:3TTN"
FT HELIX 348..361
FT /evidence="ECO:0007829|PDB:3TTN"
SQ SEQUENCE 365 AA; 40070 MW; 3F14A63C3C1D417D CRC64;
MQHSIGKTLL VAALATAIAG PVQAEKKSLH IYNWTDYIAP TTLKDFTKES GIDVSYDVFD
SNETLEGKLV SGHSGYDIVV PSNNFLGKQI QAGAFQKLDK SKLPNWKNLD PALLKQLEVS
DPGNQYAVPY LWGTNGIGYN VAKVKEVLGD QPIDSWAILF EPENMKKLAK CGVAFMDSGD
EMLPAALNYL GLDPNTHDPK DYKKAEEVLT KVRPYVSYFH SSKYISDLAN GNICVAFGYS
GDVFQAAARA EEAGKGIDIQ YVIPKEGANL WFDLMAIPAD AKAADNAYAF IDYLLRPEVI
AKVSDYVGYA NAIPGARPLM DKSVSDSEEV YPPQAVLDKL YVSAVLPAKV LRLQTRTWTR
IKTGK
