(data stored in SCRATCH zone)

SWISSPROT: C3MGL1_SINFN

ID   C3MGL1_SINFN            Unreviewed;       364 AA.
AC   C3MGL1;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 44.
DE   RecName: Full=Putrescine-binding periplasmic protein {ECO:0000256|PIRNR:PIRNR019574};
GN   OrderedLocusNames=NGR_c03280 {ECO:0000313|EMBL:ACP24126.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24126.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24126.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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|PIRNR:PIRNR019574}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein
CC       PotD/PotF family. {ECO:0000256|PIRNR:PIRNR019574}.
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DR   EMBL; CP001389; ACP24126.1; -; Genomic_DNA.
DR   RefSeq; WP_012706911.1; NC_012587.1.
DR   RefSeq; YP_002824879.1; NC_012587.1.
DR   ProteinModelPortal; C3MGL1; -.
DR   STRING; 394.NGR_c03280; -.
DR   EnsemblBacteria; ACP24126; ACP24126; NGR_c03280.
DR   GeneID; 7791554; -.
DR   KEGG; rhi:NGR_c03280; -.
DR   PATRIC; fig|394.7.peg.3131; -.
DR   eggNOG; ENOG4108HM3; Bacteria.
DR   eggNOG; ENOG410XP83; LUCA.
DR   HOGENOM; HOG000263815; -.
DR   KO; K11073; -.
DR   OMA; NWAEYID; -.
DR   OrthoDB; POG091H05D9; -.
DR   Proteomes; UP000001054; 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   InterPro; IPR001188; Sperm_putr-bd.
DR   PIRSF; PIRSF019574; Periplasmic_polyamine_BP; 1.
DR   PRINTS; PR00909; SPERMDNBNDNG.
PE   3: Inferred from homology;
DR   PRODOM; C3MGL1.
DR   SWISS-2DPAGE; C3MGL1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Periplasm {ECO:0000256|PIRNR:PIRNR019574};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transport {ECO:0000256|PIRNR:PIRNR019574}.
FT   SIGNAL        1     23       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        24    364       Putrescine-binding periplasmic protein.
FT                                {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002927809.
SQ   SEQUENCE   364 AA;  40445 MW;  3773CAA91649B788 CRC64;
     MSKFIVATLA AAMLAGSATL ASAQERVVNV YNWSDYIDES ILEEFTKETG IKVVYDVFDS
     NEILETKLLA GGSGYDVVVP TAYFLQRQIA AGVFQKLDKS KLPNLSNMWD LILERTAKYD
     PGNEYAVDYM WGTTGIGYNV DKMKEILGTD AKPNWDVIFN PEIAAKFKDC GIHLLDSPTD
     IIPSALAYLG LNPDSHDPAD LEKAADVLLK VRPYIRKFHS SEYINALANG DICLAVGFSG
     DIFQARDRAA EAKAGVTVDY SIPAQGAQMW FDMLAMPADA PHVAEAHEFI NFMMKPEVIA
     KASNYVFYAN GNKASQQFLD REVLEDTAIY PTDDVMQKLF TVTPFEPKEQ RVLTRLWTKI
     VTGQ
//

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