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DCTP_OLEA2
ID   DCTP_OLEA2              Reviewed;         336 AA.
AC   Q312S0;
DT   07-OCT-2020, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Isethionate-binding periplasmic protein DctP {ECO:0000305|PubMed:30718429};
DE   AltName: Full=TRAP transporter, DctP solute-binding subunit {ECO:0000303|PubMed:30718429};
DE   Flags: Precursor;
GN   Name=dctP {ECO:0000303|PubMed:30718429};
GN   OrderedLocusNames=Dde_1275 {ECO:0000312|EMBL:ABB38076.1};
OS   Oleidesulfovibrio alaskensis (strain ATCC BAA-1058 / DSM 17464 / G20)
OS   (Desulfovibrio alaskensis).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Oleidesulfovibrio.
OX   NCBI_TaxID=207559;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=21685289; DOI=10.1128/jb.05400-11;
RA   Hauser L.J., Land M.L., Brown S.D., Larimer F., Keller K.L.,
RA   Rapp-Giles B.J., Price M.N., Lin M., Bruce D.C., Detter J.C., Tapia R.,
RA   Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Copeland A., Lucas S.,
RA   Nolan M., Lapidus A.L., Palumbo A.V., Wall J.D.;
RT   "Complete genome sequence and updated annotation of Desulfovibrio
RT   alaskensis G20.";
RL   J. Bacteriol. 193:4268-4269(2011).
RN   [2]
RP   FUNCTION, INDUCTION, PATHWAY, DISRUPTION PHENOTYPE, AND SUBUNIT.
RC   STRAIN=ATCC BAA-1058 / DSM 17464 / G20;
RX   PubMed=30718429; DOI=10.1073/pnas.1815661116;
RA   Peck S.C., Denger K., Burrichter A., Irwin S.M., Balskus E.P.,
RA   Schleheck D.;
RT   "A glycyl radical enzyme enables hydrogen sulfide production by the human
RT   intestinal bacterium Bilophila wadsworthia.";
RL   Proc. Natl. Acad. Sci. U.S.A. 116:3171-3176(2019).
CC   -!- FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP)
CC       transport system DctPQM involved in the uptake of isethionate (2-
CC       hydroxyethanesulfonate), which is then catabolized by enzymes encoded
CC       by adjacent genes in the locus. The DctP subunit is the solute-binding
CC       protein. Thereby is involved in an anaerobic respiration pathway that
CC       converts the sulfonate isethionate to ammonia, acetate and sulfide.
CC       {ECO:0000269|PubMed:30718429}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-hydroxyethane-1-sulfonate(out) + Na(+)(out) = 2-
CC         hydroxyethane-1-sulfonate(in) + Na(+)(in); Xref=Rhea:RHEA:64584,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:61904;
CC         Evidence={ECO:0000269|PubMed:30718429};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:64585;
CC         Evidence={ECO:0000269|PubMed:30718429};
CC   -!- PATHWAY: Organosulfur degradation; alkanesulfonate degradation.
CC       {ECO:0000269|PubMed:30718429}.
CC   -!- SUBUNIT: The complex comprises the periplasmic solute receptor protein
CC       DctP, and the fused transmembrane protein DctMQ.
CC       {ECO:0000305|PubMed:30718429}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- INDUCTION: Highly up-regulated in the presence of isethionate.
CC       {ECO:0000269|PubMed:30718429}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lose the ability to grow
CC       with isethionate as the terminal electron acceptor.
CC       {ECO:0000269|PubMed:30718429}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 7 family.
CC       {ECO:0000305}.
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DR   EMBL; CP000112; ABB38076.1; -; Genomic_DNA.
DR   RefSeq; WP_011367274.1; NC_007519.1.
DR   AlphaFoldDB; Q312S0; -.
DR   SMR; Q312S0; -.
DR   STRING; 207559.Dde_1275; -.
DR   EnsemblBacteria; ABB38076; ABB38076; Dde_1275.
DR   KEGG; dde:Dde_1275; -.
DR   eggNOG; COG1638; Bacteria.
DR   HOGENOM; CLU_036176_1_3_7; -.
DR   OMA; FTYKYAN; -.
DR   OrthoDB; 752834at2; -.
DR   UniPathway; UPA00338; -.
DR   Proteomes; UP000002710; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0046306; P:alkanesulfonate catabolic process; IEA:UniProtKB-UniPathway.
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.
DR   TIGRFAMs; TIGR00787; dctP; 1.
PE   1: Evidence at protein level;
KW   Periplasm; Reference proteome; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..336
FT                   /note="Isethionate-binding periplasmic protein DctP"
FT                   /id="PRO_5004220098"
SQ   SEQUENCE   336 AA;  37241 MW;  1ADDB430FB836FF2 CRC64;
     MKHLLKAGAL VALACIVTLT AGAQAHAAKR INIRLAHPMA PGNNVTVGYE KFKELVAEKS
     NGRVRIQLFG NCMLGSDRVT MEAAQRGTLE MASSSSPNMA NFSKQWMVFD LPYITSPEHQ
     QKLYKAIDDG ELGKKLDEIA ASIGLKPIMY SEYGYRNFVT TKKPIKTADD LKNLKVRTTD
     SPIEVAVAAA LGMAPTPISW GETYTALQQG TVDGEGNTFS LLNDAKHTEV LKYAIDSAHN
     YSMHLLMMNK AYYDSLPANV QQILTEAGRE ALTYQRSITS ELEKKAEDAF IEQGITVTRL
     SPEERAKLVE RTRPVWDKFK DDIPAELIKL VQETQQ
 
 
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