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Protein

L-cystine-binding protein FliY

Gene

fliY

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the ABC transporter complex FliY-YecC-YecS involved in L-cystine transport. The system can probably also transport L-cysteine, and it mediates accumulation of the toxic compounds L-selenaproline (SCA) and L-selenocystine (SeCys). Binds cystine (PubMed:8450713).2 Publications

Enzyme regulationi

The FliY-YecC-YecS system is inhibited by L-cystine, L-cysteine, DL-2,6-diaminopimelic acid and L-cystathionine, and is stimulated by D-cysteine.1 Publication

GO - Molecular functioni

  • cysteine transmembrane transporter activity Source: EcoCyc
  • L-cystine transmembrane transporter activity Source: EcoCyc

GO - Biological processi

  • cysteine transmembrane transport Source: GOC
  • cysteine transport Source: EcoCyc
  • L-cystine transport Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Amino-acid transport, Transport

Enzyme and pathway databases

BioCyciEcoCyc:G7039-MONOMER.
ECOL316407:JW1905-MONOMER.
RETL1328306-WGS:GSTH-6379-MONOMER.

Protein family/group databases

TCDBi3.A.1.3.10. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
L-cystine-binding protein FliYCurated
Short name:
CBP
Alternative name(s):
Protein FliY
Sulfate starvation-induced protein 7
Short name:
SSI7
Gene namesi
Name:fliY
Synonyms:yzzR
Ordered Locus Names:b1920, JW1905
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12680. fliY.

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Periplasm

Pathology & Biotechi

Disruption phenotypei

The fliY-ydjN double mutant is completely resistant to both L-selenaproline and L-selenocystine.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29293 PublicationsAdd
BLAST
Chaini30 – 266237L-cystine-binding protein FliYPRO_0000031755Add
BLAST

Proteomic databases

PaxDbiP0AEM9.
PRIDEiP0AEM9.

2D gel databases

SWISS-2DPAGEP0AEM9.

Expressioni

Inductioni

Repressed by sulfate or cysteine.1 Publication

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (YecC), two transmembrane proteins (YecS) and a solute-binding protein (FliY).Curated

Protein-protein interaction databases

BioGridi4261251. 13 interactions.
DIPiDIP-47980N.
IntActiP0AEM9. 9 interactions.
MINTiMINT-1231539.
STRINGi511145.b1920.

Structurei

3D structure databases

ProteinModelPortaliP0AEM9.
SMRiP0AEM9. Positions 34-264.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4105EAB. Bacteria.
COG0834. LUCA.
HOGENOMiHOG000031895.
InParanoidiP0AEM9.
KOiK02424.
OMAiTVKWQSI.
OrthoDBiEOG6JQH58.
PhylomeDBiP0AEM9.

Family and domain databases

InterProiIPR001320. Iontro_rcpt.
IPR018313. SBP_3_CS.
IPR001638. Solute-binding_3/MltF_N.
[Graphical view]
PfamiPF00497. SBP_bac_3. 1 hit.
[Graphical view]
SMARTiSM00062. PBPb. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
PROSITEiPS01039. SBP_BACTERIAL_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0AEM9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKLAHLGRQA LMGVMAVALV AGMSVKSFAD EGLLNKVKER GTLLVGLEGT
60 70 80 90 100
YPPFSFQGDD GKLTGFEVEF AQQLAKHLGV EASLKPTKWD GMLASLDSKR
110 120 130 140 150
IDVVINQVTI SDERKKKYDF STPYTISGIQ ALVKKGNEGT IKTADDLKGK
160 170 180 190 200
KVGVGLGTNY EEWLRQNVQG VDVRTYDDDP TKYQDLRVGR IDAILVDRLA
210 220 230 240 250
ALDLVKKTND TLAVTGEAFS RQESGVALRK GNEDLLKAVN DAIAEMQKDG
260
TLQALSEKWF GADVTK
Length:266
Mass (Da):29,039
Last modified:December 20, 2005 - v1
Checksum:i1B088DF3F34E5D47
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18539 Genomic DNA. Translation: AAC43545.1.
U00096 Genomic DNA. Translation: AAC74987.1.
AP009048 Genomic DNA. Translation: BAA15740.1.
PIRiE64955.
RefSeqiNP_416430.1. NC_000913.3.
WP_001296168.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74987; AAC74987; b1920.
BAA15740; BAA15740; BAA15740.
GeneIDi948833.
KEGGiecj:JW1905.
eco:b1920.
PATRICi32119175. VBIEscCol129921_2002.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18539 Genomic DNA. Translation: AAC43545.1.
U00096 Genomic DNA. Translation: AAC74987.1.
AP009048 Genomic DNA. Translation: BAA15740.1.
PIRiE64955.
RefSeqiNP_416430.1. NC_000913.3.
WP_001296168.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP0AEM9.
SMRiP0AEM9. Positions 34-264.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261251. 13 interactions.
DIPiDIP-47980N.
IntActiP0AEM9. 9 interactions.
MINTiMINT-1231539.
STRINGi511145.b1920.

Protein family/group databases

TCDBi3.A.1.3.10. the atp-binding cassette (abc) superfamily.

2D gel databases

SWISS-2DPAGEP0AEM9.

Proteomic databases

PaxDbiP0AEM9.
PRIDEiP0AEM9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74987; AAC74987; b1920.
BAA15740; BAA15740; BAA15740.
GeneIDi948833.
KEGGiecj:JW1905.
eco:b1920.
PATRICi32119175. VBIEscCol129921_2002.

Organism-specific databases

EchoBASEiEB2545.
EcoGeneiEG12680. fliY.

Phylogenomic databases

eggNOGiENOG4105EAB. Bacteria.
COG0834. LUCA.
HOGENOMiHOG000031895.
InParanoidiP0AEM9.
KOiK02424.
OMAiTVKWQSI.
OrthoDBiEOG6JQH58.
PhylomeDBiP0AEM9.

Enzyme and pathway databases

BioCyciEcoCyc:G7039-MONOMER.
ECOL316407:JW1905-MONOMER.
RETL1328306-WGS:GSTH-6379-MONOMER.

Miscellaneous databases

PROiP0AEM9.

Family and domain databases

InterProiIPR001320. Iontro_rcpt.
IPR018313. SBP_3_CS.
IPR001638. Solute-binding_3/MltF_N.
[Graphical view]
PfamiPF00497. SBP_bac_3. 1 hit.
[Graphical view]
SMARTiSM00062. PBPb. 1 hit.
SM00079. PBPe. 1 hit.
[Graphical view]
PROSITEiPS01039. SBP_BACTERIAL_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Escherichia coli fliAZY operon."
    Mytelka D.S., Chamberlin M.J.
    J. Bacteriol. 178:24-34(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: RP437.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "Amino acid composition and N-terminal sequence of purified cystine binding protein of Escherichia coli."
    Butler J.D., Levin S.W., Facchiano A., Miele L., Mukherjee A.B.
    Life Sci. 52:1209-1215(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-59, FUNCTION.
  6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-41.
    Strain: K12 / EMG2.
  7. "Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli."
    Quadroni M., Staudenmann W., Kertesz M.A., James P.
    Eur. J. Biochem. 239:773-781(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-39; 143-148; 183-187 AND 249-266, INDUCTION.
    Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
  8. "Susceptibility of Escherichia coli to the toxic L-proline analogue L-selenaproline is dependent on two L-cystine transport systems."
    Deutch C.E., Spahija I., Wagner C.E.
    J. Appl. Microbiol. 117:1487-1499(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, DISRUPTION PHENOTYPE.
    Strain: K12.

Entry informationi

Entry nameiFLIY_ECOLI
AccessioniPrimary (citable) accession number: P0AEM9
Secondary accession number(s): P39174
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 11, 2016
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.