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UniProtKB/Swiss-Prot entry P0AE08


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AHPC_ECOLI
Primary accession number P0AE08
Secondary accession number P26427
Integrated into Swiss-Prot on December 6, 2005
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 34)
Name and origin of the protein
Protein name Alkyl hydroperoxide reductase subunit C
Synonyms EC 1.11.1.15
Peroxiredoxin
Thioredoxin peroxidase
Alkyl hydroperoxide reductase protein C22
SCRP-23
Sulfate starvation-induced protein 8
SSI8
Gene name
Name: ahpC
OrderedLocusNames: b0605, JW0598
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
PubMed=1592833 [NCBI, ExPASy, EBI, Israel, Japan]
Smillie D.A., Hayward R.S., Suzuki T., Fujita N., Ishihama A.;
"Locations of genes encoding alkyl hydroperoxide reductase on the physical map of the Escherichia coli K-12 genome.";
J. Bacteriol. 174:3826-3827(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
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.;
"Sequence of minutes 4-25 of Escherichia coli.";
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
PROTEIN SEQUENCE OF 2-31.
DOI=10.1016/0006-291X(92)90636-Y; PubMed=1575737 [NCBI, ExPASy, EBI, Israel, Japan]
Ueshima R., Fujita N., Ishihama A.;
"Identification of Escherichia coli proteins cross-reacting with antibodies against region 2.2 peptide of RNA polymerase sigma subunit.";
Biochem. Biophys. Res. Commun. 184:634-639(1992).
[7]
PROTEIN SEQUENCE OF 2-28 AND 70-81.
STRAIN=K12 / EMG2;
DOI=10.1002/elps.1150180807; PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[8]
PROTEIN SEQUENCE OF 2-21.
STRAIN=K12;
DOI=10.1074/jbc.270.48.28635; PubMed=7499381 [NCBI, ExPASy, EBI, Israel, Japan]
Cha M.-K., Kim H.-K., Kim I.-H.;
"Thioredoxin-linked 'thiol peroxidase' from periplasmic space of Escherichia coli.";
J. Biol. Chem. 270:28635-28641(1995).
[9]
PROTEIN SEQUENCE OF 2-14.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
Pasquali C., Sanchez J.-C., Ravier F., Golaz O., Hughes G.J., Frutiger S., Paquet N., Wilkins M., Appel R.D., Bairoch A., Hochstrasser D.F.;
Submitted (SEP-1994) to UniProtKB.
[10]
PROTEIN SEQUENCE OF 2-11.
STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
DOI=10.1111/j.1432-1033.1996.0773u.x; PubMed=8774726 [NCBI, ExPASy, EBI, Israel, Japan]
Quadroni M., Staudenmann W., Kertesz M.A., James P.;
"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.";
Eur. J. Biochem. 239:773-781(1996).
[11]
PROTEIN SEQUENCE OF 2-5.
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1006/jmbi.1998.1726; PubMed=9600841 [NCBI, ExPASy, EBI, Israel, Japan]
Wilkins M.R., Gasteiger E., Tonella L., Ou K., Tyler M., Sanchez J.-C., Gooley A.A., Walsh B.J., Bairoch A., Appel R.D., Williams K.L., Hochstrasser D.F.;
"Protein identification with N and C-terminal sequence tags in proteome projects.";
J. Mol. Biol. 278:599-608(1998).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-17; LYS-93; LYS-153; LYS-169 AND LYS-171, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M800187-MCP200; PubMed=18723842 [NCBI, ExPASy, EBI, Israel, Japan]
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.;
"Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli.";
Mol. Cell. Proteomics 0:0-0(2008).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D13187; BAA02485.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U82598; AAB40806.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC73706.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35235.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C64794; JN0289.
RefSeq AP_001253.1; -.
NP_415138.1; -.
3D structure databases
HSSP P19479; 1N8J. [HSSP ENTRY / PDB]
SMR P0AE08; 2-187.
ModBase P0AE08.
Protein-protein interaction databases
IntAct P0AE08; 31.
Protein family/group databases
PeroxiBase 4830; EcoAhpC.
Enzyme and pathway databases
BioCyc EcoCyc:EG11384-MON; -.
MetaCyc:EG11384-MON; -.
2D gel databases
SWISS-2DPAGE P0AE08; -.
2DBase-Ecoli P0AE08; -.
ECO2DBASE B020.9; 6TH EDITION.
Organism-specific databases
EchoBASE EB1357; -.
EcoGene EG11384; ahpC.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
GO:0005739; Cellular component: mitochondrion (inferred from direct assay from UniProtKB).
GO:0051920; Molecular function: peroxiredoxin activity (inferred from electronic annotation from EC).
GO:0045454; Biological process: cell redox homeostasis (inferred from electronic annotation from InterPro).
GO:0055114; Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000866; AhpC-TSA.
IPR017559; Peroxiredoxin.
IPR012335; Thioredoxin_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.30.10; Thioredoxin_fold; 1.
Pfam PF00578; AhpC-TSA; 1.
Pfam graphical view of domain structure.
PROSITE PS51352; THIOREDOXIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
GeneID 945225; -.
GenomeReviews AP009048_GR; JW0598.
U00096_GR; b0605.
KEGG ecj:JW0598; -.
eco:b0605; -.
Phylogenomic databases
HOGENOM P0AE08; -.
Genome annotation databases
CMR P0AE08; b0605.
Other
ProtoNet P0AE08.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Antioxidant; Complete proteome; Direct protein sequencing; Oxidoreductase; Peroxidase; Redox-active center.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   187  186     Alkyl hydroperoxide reductase subunit C. PRO_0000135115
DOMAIN   2   157  156     Thioredoxin. 
ACT_SITE   47    47        Cysteine sulfenic acid (-SOH) intermediate (By similarity). 
MOD_RES   17    17        N6-acetyllysine. 
MOD_RES   93    93        N6-acetyllysine. 
MOD_RES   153   153        N6-acetyllysine. 
MOD_RES   169   169        N6-acetyllysine. 
MOD_RES   171   171        N6-acetyllysine. 
DISULFID   47    47        Interchain (with C-166); in linked form (By similarity). 
DISULFID   166   166        Interchain (with C-47); in linked form (By similarity). 
Sequence information
Length: 187 AA [This is the length of the unprocessed precursor] Molecular weight: 20761 Da [This is the MW of the unprocessed precursor] CRC64: 40AB796E6F5CC2D6 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSLINTKIKP FKNQAFKNGE FIEITEKDTE GRWSVFFFYP ADFTFVCPTE LGDVADHYEE 

        70         80         90        100        110        120 
LQKLGVDVYA VSTDTHFTHK AWHSSSETIA KIKYAMIGDP TGALTRNFDN MREDEGLADR 

       130        140        150        160        170        180 
ATFVVDPQGI IQAIEVTAEG IGRDASDLLR KIKAAQYVAS HPGEVCPAKW KEGEATLAPS 


LDLVGKI 

P0AE08 in FASTA format

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