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DCTP_ALBFT
ID   DCTP_ALBFT              Reviewed;         338 AA.
AC   Q21XD7;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Solute-binding protein Rfer_1840 {ECO:0000305};
DE   Flags: Precursor;
GN   OrderedLocusNames=Rfer_1840 {ECO:0000312|EMBL:ABD69566.1};
OS   Albidiferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
OS   (Rhodoferax ferrireducens).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=338969 {ECO:0000312|EMBL:ABD69566.1};
RN   [1] {ECO:0000312|Proteomes:UP000008332}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-621 / DSM 15236 / T118 {ECO:0000312|Proteomes:UP000008332};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV}
RP   X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH MALONATE, AND
RP   FUNCTION.
RX   PubMed=25540822; DOI=10.1021/bi501388y;
RA   Vetting M.W., Al-Obaidi N., Zhao S., San Francisco B., Kim J.,
RA   Wichelecki D.J., Bouvier J.T., Solbiati J.O., Vu H., Zhang X.,
RA   Rodionov D.A., Love J.D., Hillerich B.S., Seidel R.D., Quinn R.J.,
RA   Osterman A.L., Cronan J.E., Jacobson M.P., Gerlt J.A., Almo S.C.;
RT   "Experimental strategies for functional annotation and metabolism
RT   discovery: targeted screening of solute binding proteins and unbiased
RT   panning of metabolomes.";
RL   Biochemistry 54:909-931(2015).
CC   -!- FUNCTION: Solute-binding protein that binds malonate (in vitro)
CC       (PubMed:25540822). Probably part of a tripartite ATP-independent
CC       periplasmic (TRAP) transport system that mediates solute transport into
CC       the cytoplasm. {ECO:0000269|PubMed:25540822, ECO:0000305}.
CC   -!- SUBUNIT: The complex is comprised of an extracytoplasmic solute-binding
CC       protein and a heteromeric permease formed by two transmembrane
CC       proteins. {ECO:0000250|UniProtKB:P37735}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P37735}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000267; ABD69566.1; -; Genomic_DNA.
DR   RefSeq; WP_011464134.1; NC_007908.1.
DR   PDB; 4MCO; X-ray; 1.60 A; A/B/C=1-338.
DR   PDB; 4MEV; X-ray; 1.80 A; A=1-338.
DR   PDBsum; 4MCO; -.
DR   PDBsum; 4MEV; -.
DR   AlphaFoldDB; Q21XD7; -.
DR   SMR; Q21XD7; -.
DR   STRING; 338969.Rfer_1840; -.
DR   EnsemblBacteria; ABD69566; ABD69566; Rfer_1840.
DR   KEGG; rfr:Rfer_1840; -.
DR   eggNOG; COG1638; Bacteria.
DR   HOGENOM; CLU_036176_1_3_4; -.
DR   OMA; HQFPGGT; -.
DR   OrthoDB; 752834at2; -.
DR   Proteomes; UP000008332; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0071702; P:organic substance transport; IEA:UniProt.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   Gene3D; 3.40.190.170; -; 1.
DR   InterPro; IPR018389; DctP_fam.
DR   InterPro; IPR038404; TRAP_DctP_sf.
DR   PANTHER; PTHR33376; PTHR33376; 1.
DR   Pfam; PF03480; DctP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   CHAIN           26..338
FT                   /note="Solute-binding protein Rfer_1840"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_5004200133"
FT   BINDING         47
FT                   /ligand="malonate"
FT                   /ligand_id="ChEBI:CHEBI:15792"
FT                   /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT   BINDING         100
FT                   /ligand="malonate"
FT                   /ligand_id="ChEBI:CHEBI:15792"
FT                   /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT   BINDING         175
FT                   /ligand="malonate"
FT                   /ligand_id="ChEBI:CHEBI:15792"
FT                   /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT   BINDING         197
FT                   /ligand="malonate"
FT                   /ligand_id="ChEBI:CHEBI:15792"
FT                   /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT   BINDING         214..218
FT                   /ligand="malonate"
FT                   /ligand_id="ChEBI:CHEBI:15792"
FT                   /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT   BINDING         244
FT                   /ligand="malonate"
FT                   /ligand_id="ChEBI:CHEBI:15792"
FT                   /evidence="ECO:0007744|PDB:4MCO, ECO:0007744|PDB:4MEV"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           46..62
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          69..71
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           79..81
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           82..87
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          92..95
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   TURN            102..104
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           106..111
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           120..125
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           130..141
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          144..148
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          151..161
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           166..169
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           179..187
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           197..199
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           200..205
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          210..215
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           216..221
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           224..226
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          229..232
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          241..243
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          246..249
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           250..255
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           258..292
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   STRAND          296..298
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           302..314
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           316..323
FT                   /evidence="ECO:0007829|PDB:4MCO"
FT   HELIX           325..338
FT                   /evidence="ECO:0007829|PDB:4MCO"
SQ   SEQUENCE   338 AA;  36911 MW;  5FBCDB16858DE50C CRC64;
     MQRRQLLQSM GGLAASTMPF SLAFAQTSAL KISHQFPGGT IKEGDFRDRL VRNFAAEVEK
     RSKGAMKFEI YPGSSLMKTN AQFSSMRKGA LDMALIPLSY AGGEVPELNI GLMPGLVVSY
     EQAYSWKTKP VGIELTRVLQ EKGIVLISWI WQAGGVASRG KPVVEPEDAK GMKIRGGSRE
     MDMILKDAGA AVVSLPSNEI YAAMQTGAMD AAMTSSTSFI SFRLEEVAKA LTTGRTGAYW
     FMFEPLMMSK AIFDKLPKDQ RDMLMTVGAE MEKFALEAAK KDDIDVAAVY QKAGAKVVDL
     SDGTIKKWQD IARKTAWKDY GAKNEGCAKL LALAQQTL
 
 
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