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. 1998 Feb;180(3):527–537. doi: 10.1128/jb.180.3.527-537.1998

TABLE 1.

Sequence analysis of SecA fragmentsa

SecA fragment (kDa) N-terminal sequence
Generated in the presence of membrane
 Extracted from membrane
  66 14NDRT
  48 361EGVQIQNENQ
  36 1MLIKLLtKVF
9vFGSRNDRTL
14nDRTLRRMRK
  31 361EGVQIQNENQ
575SGRQGdaGS
  s29 361EGVQIQNENQ
 Recovered from supernatant
  66 9VFGSRNDRTL
14NDRTLRRMRK
  36 9VFGSRNDRTL
14NDRTLRRMRK
  s29 361EGVQIQNENQ
Generated in the absence of membrane
 In buffer containing ATP and precursor
  66 9VFGSRNDRTL
14NDRTLRRMRK
  36 9VFGSRNDRTL
14NDRTLRRMRK
  s29 361EGVQIQNENQ
 In buffer with low trypsin
  66 9VFGSRNDRTL
  50 9VFGsRNDRTL
  36 104TGEGKTLTAT
  30 644QLLEQQDVA
a

SecA fragments were generated in the presence of membranes as described in Materials and Methods and were subjected to peptide-sequencing analysis. Soluble SecA (1 mg/ml) was digested with trypsin on ice for 15 min in buffer in the presence of energy source and proOmpA (1 mg of trypsin/ml) or in the absence of energy source and proOmpA (20 μg of trypsin/ml). The resulting SecA fragments were then analyzed in the same manner as the SecA fragments generated in the presence of membranes. Identified SecA sequences are shown in single-letter code. Uppercase letters represent amino acids of the analyzed sequences which match the known SecA sequence (31), whereas lowercase letters represent unconfirmed residues.