DCTP_CHRSD
ID DCTP_CHRSD Reviewed; 336 AA.
AC Q1QUN2;
DT 16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Solute-binding protein Csal_2479 {ECO:0000305};
DE Flags: Precursor;
GN Name=dctP {ECO:0000305};
GN OrderedLocusNames=Csal_2479 {ECO:0000312|EMBL:ABE59826.1};
OS Chromohalobacter salexigens (strain ATCC BAA-138 / DSM 3043 / CIP 106854 /
OS NCIMB 13768 / 1H11).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Chromohalobacter.
OX NCBI_TaxID=290398 {ECO:0000312|EMBL:ABE59826.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-138 / DSM 3043 / CIP 106854 / NCIMB 13768 / 1H11;
RX PubMed=22675587; DOI=10.4056/sigs.2285059;
RA Copeland A., O'Connor K., Lucas S., Lapidus A., Berry K.W., Detter J.C.,
RA Del Rio T.G., Hammon N., Dalin E., Tice H., Pitluck S., Bruce D.,
RA Goodwin L., Han C., Tapia R., Saunders E., Schmutz J., Brettin T.,
RA Larimer F., Land M., Hauser L., Vargas C., Nieto J.J., Kyrpides N.C.,
RA Ivanova N., Goker M., Klenk H.P., Csonka L.N., Woyke T.;
RT "Complete genome sequence of the halophilic and highly halotolerant
RT Chromohalobacter salexigens type strain (1H11(T)).";
RL Stand. Genomic Sci. 5:379-388(2011).
RN [2] {ECO:0007744|PDB:4P1L, ECO:0007744|PDB:4P3L}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 34-336 IN COMPLEX WITH
RP GLUCURONATE, AND 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 D-glucuronate (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; CP000285; ABE59826.1; -; Genomic_DNA.
DR RefSeq; WP_011507772.1; NC_007963.1.
DR PDB; 4P1L; X-ray; 1.70 A; A/B=34-336.
DR PDB; 4P3L; X-ray; 1.80 A; A=34-336.
DR PDBsum; 4P1L; -.
DR PDBsum; 4P3L; -.
DR AlphaFoldDB; Q1QUN2; -.
DR SMR; Q1QUN2; -.
DR STRING; 290398.Csal_2479; -.
DR EnsemblBacteria; ABE59826; ABE59826; Csal_2479.
DR KEGG; csa:Csal_2479; -.
DR eggNOG; COG1638; Bacteria.
DR HOGENOM; CLU_036176_4_0_6; -.
DR OMA; KSIEHSE; -.
DR OrthoDB; 752834at2; -.
DR Proteomes; UP000000239; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR GO; GO:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
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.
DR TIGRFAMs; TIGR00787; dctP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Periplasm; Reference proteome; Signal; Sugar transport;
KW Transport.
FT SIGNAL 1..33
FT /evidence="ECO:0000255"
FT CHAIN 34..336
FT /note="Solute-binding protein Csal_2479"
FT /evidence="ECO:0000255"
FT /id="PRO_5004196113"
FT BINDING 42
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0007744|PDB:4P1L, ECO:0007744|PDB:4P3L"
FT BINDING 80
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0007744|PDB:4P1L, ECO:0007744|PDB:4P3L"
FT BINDING 156
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0007744|PDB:4P1L, ECO:0007744|PDB:4P3L"
FT BINDING 177
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0007744|PDB:4P1L, ECO:0007744|PDB:4P3L"
FT BINDING 200
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0007744|PDB:4P1L, ECO:0007744|PDB:4P3L"
FT BINDING 217..218
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0007744|PDB:4P1L, ECO:0007744|PDB:4P3L"
FT BINDING 244
FT /ligand="beta-D-glucuronate"
FT /ligand_id="ChEBI:CHEBI:85313"
FT /evidence="ECO:0007744|PDB:4P1L, ECO:0007744|PDB:4P3L"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 47..62
FT /evidence="ECO:0007829|PDB:4P1L"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:4P1L"
FT TURN 74..77
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 80..88
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:4P1L"
FT TURN 100..105
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 107..113
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:4P3L"
FT HELIX 121..128
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 131..142
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 156..162
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 203..208
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 233..240
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 244..249
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 258..292
FT /evidence="ECO:0007829|PDB:4P1L"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 303..308
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 311..320
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4P1L"
FT HELIX 325..333
FT /evidence="ECO:0007829|PDB:4P1L"
SQ SEQUENCE 336 AA; 37197 MW; 7D14D72C222589C9 CRC64;
MQTNKRLKMA SCVKAAAMLG MLLSVSISTT AQADSWRGWN IHPPSYPNGK ALESFAKEVA
EKTEGRVEPK VYHNAVLGDQ PDAIEQTRSG ALDFANFNMG PMGPIVPAAN VLSLPFIFKS
PDDMYRIMDG EIGERFADAL AEKNLIVLSW FGSGARSLYN TDHPVETPDD VEGLKVRVMN
NDLYVQMIDE MGGNATPMAY GEVYQSLKTG VIDGAENNYP SYESSGHYEV ANYYSLTEHL
ILPECLCVAK ASWEELSEKD RQAIREAAED AAKEQRALWE EGVQASKQKI LDAGVKINEV
DDKSAFQAKM QPIYDQFVQE HPELESLVTD IQDAQS
