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DSRE2_ALLVD
ID   DSRE2_ALLVD             Reviewed;         159 AA.
AC   D3RPC1;
DT   15-MAR-2017, integrated into UniProtKB/Swiss-Prot.
DT   20-APR-2010, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Sulfur carrier protein DsrE2 {ECO:0000305|PubMed:24648525};
GN   Name=dsrE2 {ECO:0000303|PubMed:24648525};
GN   OrderedLocusNames=Alvin_2601 {ECO:0000312|EMBL:ADC63511.1};
OS   Allochromatium vinosum (strain ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB
OS   10441 / D) (Chromatium vinosum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=572477;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=22675582; DOI=10.4056/sigs.2335270;
RA   Weissgerber T., Zigann R., Bruce D., Chang Y.J., Detter J.C., Han C.,
RA   Hauser L., Jeffries C.D., Land M., Munk A.C., Tapia R., Dahl C.;
RT   "Complete genome sequence of Allochromatium vinosum DSM 180(T).";
RL   Stand. Genomic Sci. 5:311-330(2011).
RN   [2]
RP   FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, SULFUR-BINDING, AND PATHWAY.
RC   STRAIN=ATCC 17899 / DSM 180 / NBRC 103801 / NCIMB 10441 / D;
RX   PubMed=24648525; DOI=10.1074/jbc.m113.536425;
RA   Stockdreher Y., Sturm M., Josten M., Sahl H.G., Dobler N., Zigann R.,
RA   Dahl C.;
RT   "New proteins involved in sulfur trafficking in the cytoplasm of
RT   Allochromatium vinosum.";
RL   J. Biol. Chem. 289:12390-12403(2014).
CC   -!- FUNCTION: Sulfur carrier protein probably involved in sulfur
CC       trafficking for oxidative dissimilatory sulfur metabolism. May be a
CC       component of a cytoplasmic sulfur relay system delivering sulfur to
CC       DsrC. Binds sulfur in the presence of sulfide in vitro.
CC       {ECO:0000269|PubMed:24648525}.
CC   -!- PATHWAY: Energy metabolism; sulfur metabolism.
CC       {ECO:0000305|PubMed:24648525}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Up-regulated under sulfur-oxidizing conditions (at mRNA
CC       level), i.e. when grown on reduced sulfur compounds such as sulfide,
CC       thiosulfate or elemental sulfur. {ECO:0000269|PubMed:24648525}.
CC   -!- DISRUPTION PHENOTYPE: A mutant strain lacking rhd_2599, tusA and dsrE2,
CC       although not viable in liquid culture, is clearly sulfur oxidation
CC       negative upon growth on solid media containing sulfide, and shows
CC       massive accumulation of intercellular sulfur globules.
CC       {ECO:0000269|PubMed:24648525}.
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DR   EMBL; CP001896; ADC63511.1; -; Genomic_DNA.
DR   RefSeq; WP_012971779.1; NC_013851.1.
DR   AlphaFoldDB; D3RPC1; -.
DR   SMR; D3RPC1; -.
DR   STRING; 572477.Alvin_2601; -.
DR   EnsemblBacteria; ADC63511; ADC63511; Alvin_2601.
DR   KEGG; alv:Alvin_2601; -.
DR   eggNOG; COG2210; Bacteria.
DR   HOGENOM; CLU_094970_1_0_6; -.
DR   OMA; LQACQMT; -.
DR   OrthoDB; 2045228at2; -.
DR   UniPathway; UPA00096; -.
DR   Proteomes; UP000001441; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0006790; P:sulfur compound metabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.1260.10; -; 1.
DR   InterPro; IPR032836; DsrE2-like.
DR   InterPro; IPR027396; DsrEFH-like.
DR   Pfam; PF13686; DrsE_2; 1.
DR   SUPFAM; SSF75169; SSF75169; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..159
FT                   /note="Sulfur carrier protein DsrE2"
FT                   /id="PRO_0000439099"
FT   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        72..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   159 AA;  17555 MW;  4597D80B1E4EFBA8 CRC64;
     MEQKKLAIIA TKGSLDWAYP PFILASTAAA LGYEVQVFFT FYGLQLLKKK PNLEVTPLGN
     PGMPMPMGMD KWFPVLGLAL PGMQGMMTAM MKQKMKSKGV ASIEELRELC QEAEVKMIAC
     QMTVDLFDMP KAEFIDGVEY AGAAAFFEFA GESDICLYI
 
 
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