SPUD_PSEAE
ID SPUD_PSEAE Reviewed; 367 AA.
AC Q9I6J1;
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=Putrescine-binding periplasmic protein SpuD;
DE Flags: Precursor;
GN Name=spuD; OrderedLocusNames=PA0300;
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 26-366 OF APOPROTEIN AND IN
RP COMPLEX WITH PUTRESCINE, FUNCTION, DISRUPTION PHENOTYPE, DISULFIDE BOND,
RP AND MUTAGENESIS OF PHE-273.
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: Putrescine-binding protein probably required for putrescine
CC uptake into cells. Binds putrescine with high affinity (KD=3 nM),
CC spermidine with relatively low affinity (KD=6.8 uM). Does not bind
CC cadaverine or spermine. Putrescine binding induces large inter-domain
CC conformational changes. {ECO:0000269|PubMed:22300763}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|PIRNR:PIRNR019574}.
CC -!- DISRUPTION PHENOTYPE: No change in type 3 secretion system (T3SS)
CC induction. {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; AAG03689.1; -; Genomic_DNA.
DR PIR; E83607; E83607.
DR RefSeq; NP_248991.1; NC_002516.2.
DR RefSeq; WP_003084299.1; NZ_QZGE01000016.1.
DR PDB; 3TTK; X-ray; 2.97 A; A/B/C=26-365.
DR PDB; 3TTM; X-ray; 2.00 A; A/B=26-366.
DR PDBsum; 3TTK; -.
DR PDBsum; 3TTM; -.
DR AlphaFoldDB; Q9I6J1; -.
DR SMR; Q9I6J1; -.
DR STRING; 287.DR97_3262; -.
DR PaxDb; Q9I6J1; -.
DR PRIDE; Q9I6J1; -.
DR EnsemblBacteria; AAG03689; AAG03689; PA0300.
DR GeneID; 880655; -.
DR KEGG; pae:PA0300; -.
DR PATRIC; fig|208964.12.peg.314; -.
DR PseudoCAP; PA0300; -.
DR HOGENOM; CLU_026974_1_4_6; -.
DR InParanoid; Q9I6J1; -.
DR OMA; CISIGWS; -.
DR PhylomeDB; Q9I6J1; -.
DR BioCyc; PAER208964:G1FZ6-302-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0019810; F:putrescine 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; Disulfide bond; Periplasm; Reference proteome; Signal;
KW Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..367
FT /note="Putrescine-binding periplasmic protein SpuD"
FT /evidence="ECO:0000255"
FT /id="PRO_0000431396"
FT BINDING 36..37
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000269|PubMed:22300763"
FT BINDING 244
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000269|PubMed:22300763"
FT BINDING 275
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000269|PubMed:22300763"
FT DISULFID 173..236
FT /evidence="ECO:0000269|PubMed:22300763"
FT MUTAGEN 273
FT /note="F->W: Significant decrease in affinity for
FT putrescine (to KD=0.75 uM)."
FT /evidence="ECO:0000269|PubMed:22300763"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 43..51
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 54..61
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:3TTM"
FT TURN 119..121
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 127..140
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 164..170
FT /evidence="ECO:0007829|PDB:3TTM"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 201..214
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 215..217
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:3TTK"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 236..241
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 242..255
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 262..264
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 270..278
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 299..309
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 313..315
FT /evidence="ECO:0007829|PDB:3TTM"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 324..327
FT /evidence="ECO:0007829|PDB:3TTM"
FT TURN 330..332
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:3TTM"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:3TTM"
FT HELIX 350..364
FT /evidence="ECO:0007829|PDB:3TTM"
SQ SEQUENCE 367 AA; 40630 MW; 8734EE5F8F9BAF94 CRC64;
MMKRFGKTLL ALTLAGSVAG MAQAADNKVL HVYNWSDYIA PDTLEKFTKE TGIKVVYDVY
DSNEVLEAKL LAGKSGYDVV VPSNSFLAKQ IKAGVYQKLD KSKLPNWKNL NKDLMHTLEV
SDPGNEHAIP YMWGTIGIGY NPDKVKAAFG DNAPVDSWDL VFKPENIQKL KQCGVSFLDS
PTEILPAALH YLGYKPDTDN PKELKAAEEL FLKIRPYVTY FHSSKYISDL ANGNICVAIG
YSGDIYQAKS RAEEAKNKVT VKYNIPKEGA GSFFDMVAIP KDAENTEGAL AFVNFLMKPE
IMAEITDVVQ FPNGNAAATP LVSEAIRNDP GIYPSEEVMK KLYTFPDLPA KTQRAMTRSW
TKIKSGK
