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Database: UniProt
Entry: F7RRB2_9GAMM
LinkDB: F7RRB2_9GAMM
Original site: F7RRB2_9GAMM 
ID   F7RRB2_9GAMM            Unreviewed;       366 AA.
AC   F7RRB2;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Putrescine-binding periplasmic protein {ECO:0000256|PIRNR:PIRNR019574};
GN   ORFNames=SOHN41_02918 {ECO:0000313|EMBL:EGM69110.1};
OS   Shewanella sp. HN-41.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=327275 {ECO:0000313|EMBL:EGM69110.1, ECO:0000313|Proteomes:UP000002956};
RN   [1] {ECO:0000313|EMBL:EGM69110.1, ECO:0000313|Proteomes:UP000002956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HN-41 {ECO:0000313|EMBL:EGM69110.1,
RC   ECO:0000313|Proteomes:UP000002956};
RX   PubMed=21868804; DOI=10.1128/JB.05578-11;
RA   Kim D.H., Jiang S., Lee J.H., Cho Y.J., Chun J., Choi S.H., Park H.S.,
RA   Hur H.G.;
RT   "Draft Genome Sequence of Shewanella sp. Strain HN-41, Which Produces
RT   Arsenic-Sulfide Nanotubes.";
RL   J. Bacteriol. 193:5039-5040(2011).
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 PotD/PotF
CC       family. {ECO:0000256|PIRNR:PIRNR019574}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGM69110.1}.
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DR   EMBL; AFOZ01000037; EGM69110.1; -; Genomic_DNA.
DR   RefSeq; WP_007650064.1; NZ_AFOZ01000037.1.
DR   AlphaFoldDB; F7RRB2; -.
DR   STRING; 327275.SOHN41_02918; -.
DR   OrthoDB; 9769319at2; -.
DR   Proteomes; UP000002956; Unassembled WGS sequence.
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   CDD; cd13659; PBP2_PotF; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR006059; SBP.
DR   InterPro; IPR001188; Sperm_putr-bd.
DR   PANTHER; PTHR30222:SF12; PUTRESCINE-BINDING PERIPLASMIC PROTEIN POTF; 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.
PE   3: Inferred from homology;
KW   Periplasm {ECO:0000256|PIRNR:PIRNR019574};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|PIRNR:PIRNR019574}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..366
FT                   /note="Putrescine-binding periplasmic protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003361022"
SQ   SEQUENCE   366 AA;  40514 MW;  39DF35896517253B CRC64;
     MKLFNKMTTL ALVTAGALAS VAAQAEEVVR VYNWSDYIAE DTLENFKKET GIRVIYDVFD
     SNEVLEAKLL SGRSGYDIVV PSNHFLAKQI KAGAFKSLDR SKLPNFKNLN AELMKQLEKA
     DPGNQYAVPY LWGTNGIGYN IDKVKAAVGE DAPFNSMELI FNPKYAEKIS KCGFAMLDSA
     DDMVPQAMIY LGLDPNSTKA EDYEKAGELL EKIRPYVTYF HSSRYISDLA NGDICVAFGF
     SGDVFQAAAR ADEAGNGNKI GYSIPKEGAN LWFDMLAIPA DATNVDNAHK LINYLLRPDV
     IAPISNYVAY ANPNDPAQPL VDEAIRNDPA IYPPKEVLDK LYIGEIRPLK VQRVLTRVWT
     KVKSGQ
//
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