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P15078 (CSTA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Carbon starvation protein A
Gene names
Name:cstA
Synonyms:ybdC
Ordered Locus Names:b0598, JW0590
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length701 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Peptide utilization during carbon starvation.

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Induction

By carbon starvation.

Sequence similarities

Belongs to the CstA family.

Sequence caution

The sequence CAA37087.1 differs from that shown. Reason: Frameshift at position 543.

Ontologies

Keywords
   Biological processStress response
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to starvation

Inferred from expression pattern Ref.1. Source: EcoCyc

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 701701Carbon starvation protein A
PRO_0000190046

Regions

Topological domain1 – 66Cytoplasmic Potential
Transmembrane7 – 2721Helical; Potential
Topological domain28 – 336Periplasmic Potential
Transmembrane34 – 5421Helical; Potential
Topological domain55 – 8632Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 11710Periplasmic Potential
Transmembrane118 – 13821Helical; Potential
Topological domain139 – 16123Cytoplasmic Potential
Transmembrane162 – 18221Helical; Potential
Topological domain183 – 1897Periplasmic Potential
Transmembrane190 – 21021Helical; Potential
Topological domain211 – 2177Cytoplasmic Potential
Transmembrane218 – 23821Helical; Potential
Topological domain239 – 25517Periplasmic Potential
Transmembrane256 – 27621Helical; Potential
Topological domain277 – 2804Cytoplasmic Potential
Transmembrane281 – 30121Helical; Potential
Topological domain302 – 32423Periplasmic Potential
Transmembrane325 – 34521Helical; Potential
Topological domain346 – 37227Cytoplasmic Potential
Transmembrane373 – 39321Helical; Potential
Topological domain394 – 3952Periplasmic Potential
Transmembrane396 – 41621Helical; Potential
Topological domain417 – 43923Cytoplasmic Potential
Transmembrane440 – 46021Helical; Potential
Topological domain461 – 4633Periplasmic Potential
Transmembrane464 – 48421Helical; Potential
Topological domain485 – 52339Cytoplasmic Potential
Transmembrane524 – 54421Helical; Potential
Topological domain545 – 5506Periplasmic Potential
Transmembrane551 – 57121Helical; Potential
Topological domain572 – 5776Cytoplasmic Potential
Transmembrane578 – 59821Helical; Potential
Topological domain599 – 64345Periplasmic Potential
Transmembrane644 – 66421Helical; Potential
Topological domain665 – 70137Cytoplasmic Potential

Experimental info

Sequence conflict1291A → G in CAA37086. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P15078 [UniParc].

Last modified November 1, 1997. Version 3.
Checksum: 2DA85B2D96FD19E5

FASTA70175,105
        10         20         30         40         50         60 
MNKSGKYLVW TVLSVMGAFA LGYIALNRGE QINALWIVVA SVCIYLIAYR FYGLYIAKNV 

        70         80         90        100        110        120 
LAVDPTRMTP AVRHNDGLDY VPTDKKVLFG HHFAAIAGAG PLVGPVLAAQ MGYLPGMIWL 

       130        140        150        160        170        180 
LAGVVLAGAV QDFMVLFVST RRDGRSLGEL VKEEMGPTAG VIALVACFMI MVIILAVLAM 

       190        200        210        220        230        240 
IVVKALTHSP WGTYTVAFTI PLALFMGIYL RYLRPGRIGE VSVIGLVFLI FAIISGGWVA 

       250        260        270        280        290        300 
ESPTWAPYFD FTGVQLTWML VGYGFVAAVL PVWLLLAPRD YLSTFLKIGT IVGLAVGILI 

       310        320        330        340        350        360 
MRPTLTMPAL TKFVDGTGPV WTGNLFPFLF ITIACGAVSG FHALISSGTT PKMLANEGQA 

       370        380        390        400        410        420 
CFIGYGGMLM ESFVAIMALV SACIIDPGVY FAMNSPMAVL APAGTADVVA SAAQVVSSWG 

       430        440        450        460        470        480 
FSITPDTLNQ IASEVGEQSI ISRAGGAPTL AVGMAYILHG ALGGMMDVAF WYHFAILFEA 

       490        500        510        520        530        540 
LFILTAVDAG TRAARFMLQD LLGVVSPGLK RTDSLPANLL ATALCVLAWG YFLHQGVVDP 

       550        560        570        580        590        600 
LGGINTLWPL FGIANQMLAG MALMLCAVVL FKMKRQRYAW VALVPTAWLL ICTLTAGWQK 

       610        620        630        640        650        660 
AFSPDAKVGF LAIANKFQAM IDSGNIPSQY TESQLAQLVF NNRLDAGLTI FFMVVVVVLA 

       670        680        690        700 
LFSIKTALAA LKDPKPTAKE TPYEPMPENV EEIVAQAKGA H 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and functional characterization of a carbon starvation gene of Escherichia coli."
Schultz J.E., Matin A.
J. Mol. Biol. 218:129-140(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
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]"Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase."
Liu J., Duncan K., Walsh C.T.
J. Bacteriol. 171:791-798(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200.
[6]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52904 Genomic DNA. Translation: CAA37086.1. Frameshift.
X52904 Genomic DNA. Translation: CAA37087.1. Frameshift.
U82598 Genomic DNA. Translation: AAB40798.1.
U00096 Genomic DNA. Translation: AAC73699.1.
AP009048 Genomic DNA. Translation: BAA35227.1.
M24148 Unassigned DNA. No translation available.
PIRQ0ECNA. D64793.
RefSeqNP_415130.1. NC_000913.2.
YP_488887.1. NC_007779.1.

3D structure databases

ProteinModelPortalP15078.
ModBaseSearch...

Protein-protein interaction databases

STRING511145.b0598.

Protein family/group databases

TCDB9.B.59.1.1. putative peptide transporter carbon starvation CstA family.

Proteomic databases

PaxDbP15078.
PRIDEP15078.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73699; AAC73699; b0598.
BAA35227; BAA35227; BAA35227.
GeneID12931991.
945213.
KEGGecj:Y75_p0587.
eco:b0598.
PATRIC32116372. VBIEscCol129921_0626.

Organism-specific databases

EchoBASEEB0165.
EcoGeneEG10167. cstA.

Phylogenomic databases

eggNOGCOG1966.
HOGENOMHOG000220271.
KOK06200.
OMAVVLFKMG.
ProtClustDBPRK15015.

Enzyme and pathway databases

BioCycEcoCyc:EG10167-MONOMER.
ECOL316407:JW0590-MONOMER.

Gene expression databases

GenevestigatorP15078.

Family and domain databases

InterProIPR003706. C_starv_induced_CstA.
IPR025299. CstA_C.
[Graphical view]
PfamPF02554. CstA. 1 hit.
PF13722. DUF4161. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCSTA_ECOLI
AccessionPrimary (citable) accession number: P15078
Secondary accession number(s): P23517, P77740
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families