cstA:Gene Product(s)

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Nomenclature Function Interactions Localization Sequence Domains Structure Resources Accessions Links References Suggestions

Nomenclature

Standard name

CstA product

Synonyms

carbon starvation protein product[1], B0598 product[2][1], YbdC product[2][1], CstA product[2][1]

Product description

peptide transporter induced by carbon starvation[2][3]

EC number (for enzymes)
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Notes

Function

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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.

Qualifier GO ID GO term name Reference(s) Evidence Code with/from Aspect Notes Status
GO:0006950

response to stress

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0346

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0009267

cellular response to starvation

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR003706

P

Seeded from EcoCyc 12.5 [4]

complete

GO:0016020

membrane

GO_REF:0000002
GO_REF:0000004
GO_REF:0000004

IEA: Inferred from Electronic Annotation

InterPro:IPR003706
SP_KW:KW-0397
SP_KW:KW-0472

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0016021

integral to membrane

GO_REF:0000004

IEA: Inferred from Electronic Annotation

SP_KW:KW-0812

C

Seeded from EcoCyc 12.5 [4]

complete

GO:0006810

transport

P

Seeded from EcoCyc 11.1[3].

required fields missing

GO:0042594

response to starvation

P

Seeded from EcoCyc 11.1[3].

required fields missing

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Interactions

Partner Type Partner Notes References
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Notes

Localization

Compartment Description Evidence Notes

plasma membrane

C-terminus localized in the cytoplasm with 18 predicted transmembrane domains

Daley et al. (2005) [5]


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Notes

Structure and Physical Properties

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Physical Properties

Sequence

at EcoCyc

MNKSGKYLVW TVLSVMGAFA LGYIALNRGE QINALWIVVA SVCIYLIAYR FYGLYIAKNV
LAVDPTRMTP AVRHNDGLDY VPTDKKVLFG HHFAAIAGAG PLVGPVLAAQ MGYLPGMIWL
LAGVVLAGAV QDFMVLFVST RRDGRSLGEL VKEEMGPTAG VIALVACFMI MVIILAVLAM
IVVKALTHSP WGTYTVAFTI PLALFMGIYL RYLRPGRIGE VSVIGLVFLI FAIISGGWVA
ESPTWAPYFD FTGVQLTWML VGYGFVAAVL PVWLLLAPRD YLSTFLKIGT IVGLAVGILI
MRPTLTMPAL TKFVDGTGPV WTGNLFPFLF ITIACGAVSG FHALISSGTT PKMLANEGQA
CFIGYGGMLM ESFVAIMALV SACIIDPGVY FAMNSPMAVL APAGTADVVA SAAQVVSSWG
FSITPDTLNQ IASEVGEQSI ISRAGGAPTL AVGMAYILHG ALGGMMDVAF WYHFAILFEA
LFILTAVDAG TRAARFMLQD LLGVVSPGLK RTDSLPANLL ATALCVLAWG YFLHQGVVDP
LGGINTLWPL FGIANQMLAG MALMLCAVVL FKMKRQRYAW VALVPTAWLL ICTLTAGWQK
AFSPDAKVGF LAIANKFQAM IDSGNIPSQY TESQLAQLVF NNRLDAGLTI FFMVVVVVLA
LFSIKTALAA LKDPKPTAKE TPYEPMPENV EEIVAQAKGA H
Mol. Wt

75.11 kDa (calc) [2]

pI
Extinction coefficient

120780 - 121780 (calc based on 22 Y, 16 W, and 8 C residues)

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Domains/Motifs/Modification Sites

Type Residues Description Notes

Domain

441 - 463

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

468 - 487

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

514 - 533

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

548 - 570

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

577 - 599

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

649 - 671

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

7 - 26

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

32 - 54

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

89 - 111

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

116 - 138

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

159 - 181

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

191 - 213

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

218 - 240

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

255 - 277

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

284 - 306

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

326 - 348

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

361 - 383

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

Domain

398 - 420

Predicted membrane-spanning helix.

TMD predicted by TMHMM[6]

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tmhmm.php?gene=cstA&show=pic&.jpg
Click the image to view raw output from TMHMM.

Structure

Structures

<beststructure>cstA 562</beststructure>

Models

View models at:

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Notes

Gene Product Resources

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Resource type Source Notes/Reference
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Notes

Accessions in Other Databases

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Database Accession Notes

EcoCyc (EcoliWiki Page)

EcoCyc:EG10167-MONOMER

UniProt (EcoliWiki Page)

UniProt:P15078

PFAM (EcoliWiki Page)

PFAM:PF02554

RefSeq (EcoliWiki Page)

RefSeq:NP_415130


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Notes

Links

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Name URL Comments
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References

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See Help:References for how to manage references in EcoliWiki.

  1. ↑ 1.0 1.1 1.2 1.3 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
  2. ↑ 2.0 2.1 2.2 2.3 2.4 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. ↑ 3.0 3.1 3.2 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  4. ↑ 4.0 4.1 4.2 4.3 EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  5. ↑ Daley, DO et al. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308 1321-3 PubMed
  6. ↑ 6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10 6.11 6.12 6.13 6.14 6.15 6.16 6.17 Krogh, A et al. (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J. Mol. Biol. 305 567-80 PubMed


Categories

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