DCTP_SULSN
ID DCTP_SULSN Reviewed; 330 AA.
AC A3T0D1;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Solute-binding protein NAS141_03721 {ECO:0000305};
DE Flags: Precursor;
GN ORFNames=NAS141_03721 {ECO:0000312|EMBL:EAP79685.1};
OS Sulfitobacter sp. (strain NAS-14.1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=314267;
RN [1] {ECO:0000312|Proteomes:UP000004141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAS-14.1 {ECO:0000312|Proteomes:UP000004141};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:4NX1, ECO:0007744|PDB:4OVP}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 28-330 IN COMPLEXES WITH
RP ALPHA-D-MANNURONATE AND ALPHA-D-TALURONATE.
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 D-mannuronate and D-
CC taluronate (in vitro) (PubMed:25540822). Probably part of a tripartite
CC ATP-independent periplasmic (TRAP) transport system that mediates
CC solute transport into the cytoplasm. {ECO:0000269|PubMed:25540822,
CC 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; AALZ01000007; EAP79685.1; -; Genomic_DNA.
DR RefSeq; WP_009824394.1; NZ_AALZ01000007.1.
DR PDB; 4NX1; X-ray; 1.60 A; A/B=28-330.
DR PDB; 4OVP; X-ray; 1.70 A; A/B=28-330.
DR PDBsum; 4NX1; -.
DR PDBsum; 4OVP; -.
DR AlphaFoldDB; A3T0D1; -.
DR SMR; A3T0D1; -.
DR HOGENOM; CLU_036176_4_1_5; -.
DR Proteomes; UP000004141; Unassembled WGS sequence.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
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; IPR004682; TRAP_DctP.
DR InterPro; IPR038404; TRAP_DctP_sf.
DR PANTHER; PTHR33376; PTHR33376; 1.
DR Pfam; PF03480; DctP; 1.
DR PIRSF; PIRSF006470; DctB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Signal; Transport.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT CHAIN 28..330
FT /note="Solute-binding protein NAS141_03721"
FT /evidence="ECO:0000255"
FT /id="PRO_5002659887"
FT BINDING 75
FT /ligand="alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:157625"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OVP"
FT BINDING 75
FT /ligand="alpha-D-taluronate"
FT /ligand_id="ChEBI:CHEBI:157627"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4NX1"
FT BINDING 97
FT /ligand="alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:157625"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OVP"
FT BINDING 97
FT /ligand="alpha-D-taluronate"
FT /ligand_id="ChEBI:CHEBI:157627"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4NX1"
FT BINDING 153
FT /ligand="alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:157625"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OVP"
FT BINDING 153
FT /ligand="alpha-D-taluronate"
FT /ligand_id="ChEBI:CHEBI:157627"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4NX1"
FT BINDING 173
FT /ligand="alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:157625"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OVP"
FT BINDING 173
FT /ligand="alpha-D-taluronate"
FT /ligand_id="ChEBI:CHEBI:157627"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4NX1"
FT BINDING 196
FT /ligand="alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:157625"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OVP"
FT BINDING 196
FT /ligand="alpha-D-taluronate"
FT /ligand_id="ChEBI:CHEBI:157627"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4NX1"
FT BINDING 213..214
FT /ligand="alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:157625"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OVP"
FT BINDING 213..214
FT /ligand="alpha-D-taluronate"
FT /ligand_id="ChEBI:CHEBI:157627"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4NX1"
FT BINDING 240
FT /ligand="alpha-D-mannuronate"
FT /ligand_id="ChEBI:CHEBI:157625"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4OVP"
FT BINDING 240
FT /ligand="alpha-D-taluronate"
FT /ligand_id="ChEBI:CHEBI:157627"
FT /evidence="ECO:0000269|PubMed:25540822,
FT ECO:0007744|PDB:4NX1"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 42..57
FT /evidence="ECO:0007829|PDB:4NX1"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:4NX1"
FT TURN 69..72
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:4NX1"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4NX1"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 130..140
FT /evidence="ECO:0007829|PDB:4NX1"
FT STRAND 142..159
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4NX1"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 178..186
FT /evidence="ECO:0007829|PDB:4NX1"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 196..198
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:4NX1"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 215..220
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:4NX1"
FT STRAND 229..245
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 246..251
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 254..288
FT /evidence="ECO:0007829|PDB:4NX1"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:4NX1"
FT TURN 298..301
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 302..317
FT /evidence="ECO:0007829|PDB:4NX1"
FT HELIX 321..327
FT /evidence="ECO:0007829|PDB:4NX1"
SQ SEQUENCE 330 AA; 36019 MW; 6EFBD2907BE68AA0 CRC64;
MSFFTKTAQL VSGAAVAATL FTATAQAETV LRGASMFDEE HAFTKTLRKF EELVDEKYDG
DVTFDLRLNG ELGVESDYVT FLNQGVAIDY TILAPSNMAK FAPSIPLMDM PFLFRDLDHW
NAVLSSDVLA PLEDELLEKA DIKIVGYTGG GTRNLLSKQP VVTFDDLKGH KMRVMGAPIQ
AQIFQALTAA PSAIAYNEVY NAIQTGVIAG FENEAASIQN LKFYEVAPNL TLTRHSITVR
PIVMSGKTFN SLPADLQAVV LEAGEEAGAY GRELESREDG VKLQEMVDAG QLTVSEFENR
DKMLEMVKPV QDAYAAEIGA SDLLEAVRAK
