ID W0BDV3_9GAMM Unreviewed; 345 AA.
AC W0BDV3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Putrescine-binding periplasmic protein {ECO:0000256|PIRNR:PIRNR019574};
GN ORFNames=Loa_01228 {ECO:0000313|EMBL:AHE66782.1};
OS Legionella oakridgensis ATCC 33761 = DSM 21215.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE66782.1, ECO:0000313|Proteomes:UP000018838};
RN [1] {ECO:0000313|EMBL:AHE66782.1, ECO:0000313|Proteomes:UP000018838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA Heuner K.;
RT "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT characterization reveals its replication capacity in amoebae.";
RL Int. J. Med. Microbiol. 303:514-528(2013).
CC -!- FUNCTION: Required for the activity of the bacterial periplasmic
CC transport system of putrescine. {ECO:0000256|PIRNR:PIRNR019574}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418,
CC ECO:0000256|PIRNR:PIRNR019574}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 family.
CC {ECO:0000256|ARBA:ARBA00008520}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein PotD/PotF
CC family. {ECO:0000256|PIRNR:PIRNR019574}.
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DR EMBL; CP004006; AHE66782.1; -; Genomic_DNA.
DR RefSeq; WP_025385476.1; NZ_CP004006.1.
DR AlphaFoldDB; W0BDV3; -.
DR STRING; 1268635.Loa_01228; -.
DR KEGG; lok:Loa_01228; -.
DR PATRIC; fig|1268635.3.peg.1234; -.
DR eggNOG; COG0687; Bacteria.
DR HOGENOM; CLU_026974_1_3_6; -.
DR Proteomes; UP000018838; Chromosome.
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 GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd13590; PBP2_PotD_PotF_like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR006059; SBP.
DR InterPro; IPR006061; SBP_1_CS.
DR InterPro; IPR001188; Sperm_putr-bd.
DR PANTHER; PTHR30222:SF17; BIFUNCTIONAL POLYHYDROXYBUTYRATE SYNTHASE _ ABC TRANSPORTER PERIPLASMIC BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR30222; SPERMIDINE/PUTRESCINE-BINDING PERIPLASMIC PROTEIN; 1.
DR Pfam; PF13416; SBP_bac_8; 1.
DR PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1.
DR PRINTS; PR00909; SPERMDNBNDNG.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS01037; SBP_BACTERIAL_1; 1.
PE 3: Inferred from homology;
KW Periplasm {ECO:0000256|PIRNR:PIRNR019574};
KW Reference proteome {ECO:0000313|Proteomes:UP000018838};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR019574}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..345
FT /note="Putrescine-binding periplasmic protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004786005"
FT BINDING 82
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|PIRSR:PIRSR019574-1"
FT BINDING 164..167
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|PIRSR:PIRSR019574-1"
FT BINDING 323
FT /ligand="spermidine"
FT /ligand_id="ChEBI:CHEBI:57834"
FT /evidence="ECO:0000256|PIRSR:PIRSR019574-1"
SQ SEQUENCE 345 AA; 39650 MW; 409A8F717B0626FA CRC64;
MKQSIRTFFL LLIVLFTAPT YANNVVNVYV WGGEIPKSLI HQFERETGIK VNFSTYDSNE
TMYAKLKASR QSVYDVIMPS GYYVERMKKQ GMLTKLTHDK IPNLDNIDPL FTKSQYDAGN
HYSVPLTWGA TGIFYNTQWV HDIPKKWSDL WEKRWHRQLL LLDDSREVFS IALMSLGYHP
NDKNPAHIQQ AYEQLLALVP NIKLFASDSV QAIIIDEDAI AGSAWNGDAY KAQAENKQIH
FIYPKEGYVI WVGCLSIPNH PPHPKEAYAF INFMLKPSSA VQIALREGHA ITNAKGKALL
PDTIRHNPMI YPSQETLKRG YFQQDVGDKT IALYNQYWEQ LKLSF
//