SPUD_PSEAB
ID SPUD_PSEAB Reviewed; 367 AA.
AC Q02UB7;
DT 07-JAN-2015, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Putrescine-binding periplasmic protein SpuD;
DE Flags: Precursor;
GN Name=spuD; OrderedLocusNames=PA14_03920;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RC STRAIN=UCBPP-PA14;
RX PubMed=24965220; DOI=10.1002/pmic.201400190;
RA Ouidir T., Jarnier F., Cosette P., Jouenne T., Hardouin J.;
RT "Extracellular Ser/Thr/Tyr phosphorylated proteins of Pseudomonas
RT aeruginosa PA14 strain.";
RL Proteomics 14:2017-2030(2014).
CC -!- FUNCTION: Putrescine-binding protein probably required for putrescine
CC uptake into cells. Binds putrescine with high affinity, spermidine with
CC relatively low affinity. Does not bind cadaverine or spermine.
CC Putrescine binding induces large inter-domain conformational changes.
CC {ECO:0000250|UniProtKB:Q9I6J1}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|PIRNR:PIRNR019574}.
CC Secreted {ECO:0000269|PubMed:24965220}. Note=Could be present
CC extracellularly due to cell outer membrane leakage. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein PotD/PotF
CC family. {ECO:0000255|PIRNR:PIRNR019574}.
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DR EMBL; CP000438; ABJ15262.1; -; Genomic_DNA.
DR RefSeq; WP_003084299.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02UB7; -.
DR SMR; Q02UB7; -.
DR PRIDE; Q02UB7; -.
DR EnsemblBacteria; ABJ15262; ABJ15262; PA14_03920.
DR KEGG; pau:PA14_03920; -.
DR HOGENOM; CLU_026974_1_4_6; -.
DR OMA; CISIGWS; -.
DR BioCyc; PAER208963:G1G74-328-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0019808; F:polyamine binding; IEA:InterPro.
DR GO; GO:0015846; P:polyamine transport; IEA:InterPro.
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 Disulfide bond; Periplasm; Secreted; Signal; 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_0000431395"
FT BINDING 36..37
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250|UniProtKB:Q9I6J1"
FT BINDING 244
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250|UniProtKB:Q9I6J1"
FT BINDING 275
FT /ligand="putrescine"
FT /ligand_id="ChEBI:CHEBI:326268"
FT /evidence="ECO:0000250|UniProtKB:Q9I6J1"
FT DISULFID 173..236
FT /evidence="ECO:0000250|UniProtKB:Q9I6J1"
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