Identification
Name:Probable ATP-dependent transporter sufC
Synonyms:Not Available
Gene Name:sufC
Enzyme Class:Not Available
Biological Properties
General Function:Involved in nucleotide binding
Specific Function:Has low ATPase activity. The sufBCD complex acts synergistically with sufE to stimulate the cysteine desulfurase activity of sufS. The sufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation
Cellular Location:Cytoplasm
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
Complex Reactions:
1.0[2Fe-1S] desulfurated iron-sulfur cluster+1.0Thumb+1.0Thumb+1.0SufBCD scaffold complex+1.0SufSE with bound sulfur1.0Thumb+5.0Thumb+1.0Thumb+1.0SufBCD with bound [2Fe-2S] cluster+1.0SufSE sulfur acceptor complex
1.0[2Fe-1S] desulfurated iron-sulfur cluster + 1.0Adenosine triphosphate + 1.0Water + 1.0SufBCD scaffold complex + 1.0SufSE with bound sulfur → 1.0ADP + 5.0Hydrogen ion + 1.0Phosphate + 1.0SufBCD with bound [2Fe-2S] cluster + 1.0SufSE sulfur acceptor complex
ReactionCard
1.0Thumb+2.0Thumb+1.0SufBCD with two bound [2Fe-2S] clusters1.0Thumb+1.0SufBCD with bound [4Fe-4S] cluster
1.0FADH2 + 2.0Hydrogen ion + 1.0SufBCD with two bound [2Fe-2S] clusters → 1.0FAD + 1.0SufBCD with bound [4Fe-4S] cluster
ReactionCard
4.0Thumb+1.0SufBCD with bound [2Fe-2S] cluster1.0[2Fe-2S] iron-sulfur cluster+1.0SufBCD scaffold complex
4.0Hydrogen ion + 1.0SufBCD with bound [2Fe-2S] cluster → 1.0[2Fe-2S] iron-sulfur cluster + 1.0SufBCD scaffold complex
ReactionCard
4.0Thumb+1.0SufBCD with bound [4Fe-4S] cluster1.0[4Fe-4S] iron-sulfur cluster+1.0SufBCD scaffold complex
4.0Hydrogen ion + 1.0SufBCD with bound [4Fe-4S] cluster → 1.0[4Fe-4S] iron-sulfur cluster + 1.0SufBCD scaffold complex
ReactionCard
1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb+1.0SufBCD scaffold complex+2.0SufSE with bound sulfur1.0Thumb+1.0Thumb+7.0Thumb+1.0Thumb+1.0SufBCD with bound [2Fe-2S] cluster+2.0SufSE sulfur acceptor complex
1.0Adenosine triphosphate + 1.0FADH2 + 2.0Iron + 1.0Water + 1.0SufBCD scaffold complex + 2.0SufSE with bound sulfur → 1.0ADP + 1.0FAD + 7.0Hydrogen ion + 1.0Phosphate + 1.0SufBCD with bound [2Fe-2S] cluster + 2.0SufSE sulfur acceptor complex
ReactionCard
1.0Thumb+1.0Thumb+2.0Thumb+1.0Thumb+1.0SufBCD with bound [2Fe-2S] cluster+2.0SufSE with bound sulfur1.0Thumb+1.0Thumb+7.0Thumb+1.0Thumb+1.0SufBCD with two bound [2Fe-2S] clusters+2.0SufSE sulfur acceptor complex
1.0Adenosine triphosphate + 1.0FADH2 + 2.0Iron + 1.0Water + 1.0SufBCD with bound [2Fe-2S] cluster + 2.0SufSE with bound sulfur → 1.0ADP + 1.0FAD + 7.0Hydrogen ion + 1.0Phosphate + 1.0SufBCD with two bound [2Fe-2S] clusters + 2.0SufSE sulfur acceptor complex
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB01248FADMetaboCard
ECMDB01197FADH2MetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00692IronMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
ATPase activity
binding
catalytic activity
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
nucleoside binding
nucleoside-triphosphatase activity
nucleotide binding
purine nucleoside binding
pyrophosphatase activity
Process
establishment of localization
transport
Gene Properties
Blattner:b1682
Gene OrientationCounterclockwise
Centisome Percentage:37.93
Left Sequence End1759790
Right Sequence End1760536
Gene Sequence:
>747 bp
ATGGATTTCAGCGGTAAAAATGTCTGGGTAACCGGCGCAGGTAAAGGTATCGGCTACGCC
ACGGCGCTGGCGTTTGTTGAGGCGGGAGCGAAAGTTACAGGTTTTGATCAAGCGTTCACT
CAGGAGCAATATCCCTTTGCGACCGAAGTGATGGATGTTGCCGACGCTGCGCAGGTCGCG
CAAGTGTGTCAGCGACTGTTAGCTGAAACGGAGCGACTGGACGCGCTGGTCAATGCGGCG
GGAATTTTACGCATGGGCGCGACCGATCAGCTCAGTAAAGAGGACTGGCAGCAGACTTTT
GCGGTTAACGTCGGCGGTGCGTTTAACCTGTTCCAGCAAACCATGAACCAGTTTCGCCGT
CAGCGGGGCGGGGCGATTGTCACTGTGGCGTCCGACGCCGCGCACACGCCGCGTATTGGC
ATGAGTGCTTATGGCGCATCGAAAGCGGCGCTGAAAAGCCTGGCGTTGAGCGTCGGGCTG
GAACTGGCGGGTAGCGGCGTGCGCTGTAATGTGGTTTCGCCTGGCTCCACCGACACCGAT
ATGCAACGCACGCTGTGGGTGAGCGATGACGCCGAAGAACAGCGTATTCGCGGCTTTGGC
GAGCAGTTTAAACTCGGCATTCCGCTGGGGAAAATCGCCCGTCCACAAGAGATCGCCAAC
ACGATTTTGTTCCTCGCCTCTGACCTCGCCAGCCATATTACCCTACAGGATATTGTGGTC
GATGGCGGCTCAACGCTGGGGGCATAA
Protein Properties
Pfam Domain Function:
Protein Residues:248
Protein Molecular Weight:27582
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Probable ATP-dependent transporter sufC
MLSIKDLHVSVEDKAILRGLSLDVHPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTV
EFKGKDLLALSPEDRAGEGIFMAFQYPVEIPGVSNQFFLQTALNAVRSYRGQETLDRFDF
QDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELCILDESDSGLDIDA
LKVVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQG
YGWLTEQQ
References
External Links:
ResourceLink
Uniprot ID:P77499
Uniprot Name:SUFC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674717
Ecogene ID:EG13964
Ecocyc:EG13964
ColiBase:b1682
Kegg Gene:b1682
EchoBASE ID:EB3722
CCDB:SUFC_ECOLI
BacMap:16129638
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kitaoka, S., Wada, K., Hasegawa, Y., Minami, Y., Fukuyama, K., Takahashi, Y. (2006). "Crystal structure of Escherichia coli SufC, an ABC-type ATPase component of the SUF iron-sulfur cluster assembly machinery." FEBS Lett 580:137-143. Pubmed: 16364320
  • Nachin, L., Loiseau, L., Expert, D., Barras, F. (2003). "SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress." EMBO J 22:427-437. Pubmed: 12554644
  • Outten, F. W., Wood, M. J., Munoz, F. M., Storz, G. (2003). "The SufE protein and the SufBCD complex enhance SufS cysteine desulfurase activity as part of a sulfur transfer pathway for Fe-S cluster assembly in Escherichia coli." J Biol Chem 278:45713-45719. Pubmed: 12941942
  • Patzer, S. I., Hantke, K. (1999). "SufS is a NifS-like protein, and SufD is necessary for stability of the [2Fe-2S] FhuF protein in Escherichia coli." J Bacteriol 181:3307-3309. Pubmed: 10322040