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. 1998 Apr;180(7):1904–1912. doi: 10.1128/jb.180.7.1904-1912.1998

TABLE 1.

Putative export signals of ΔSPNuc fusions in L. lactis

ΔSPNuc fusion Sizea Putative export signal sequencesb
Exp polypeptides
 Exp1c 320           MKNLIPKKIKQVGILVGALLMLLSVLPVNLLGVMKVDA↓DSSQTEV-275
 Exp2c 284                        MKKIAIIFCTLLMSLSVLSSFAVSA↓DTTTTNN-252
 Exp3 92                    VEKVKHEKGIIAFLTVLTILLTGAVKVSA↓DSTQAEI-56 
 Exp4 144                        MKKINLALLTLATLMGVSSTAVVFA↓DDATSTG-112
 Exp5 455 VRYSKISTKSKKNKQNKRAKRGSAKSKWWTAVKLFLIVFFSLIILGLA↓AGGAVFV-400
Nlp polypeptides
 Nlp1c 140                             MKKKIFIALMASVSLFTLAA↓CGSGNKQ-113
 Nlp2c 91                           MKSWKKVALGGASVLALATLAA↓CGSSASS-62 
 Nlp3 110                               MKKILMLFAIPAVLLLAG↓CQKTADK-85 
 Nlp4 94                         LKFKKLGLVMATVFAGAALVTLSG↓CSSSDSA-63 
Tmp polypeptides
 Tmp1 40                        MKLKHIMLMTVLYIIATLSLVILSNQNILENDT-7  
 Tmp2 111              48-KFKKFSGVEKVFYLTMVVAALVLAVGLLYVKTKTLEVQGN-23 
 Tmp3 196         28-LSITFKVLRGLSVVFGIVFVLVGVFGAATGVGYFARLVEQTKIPP-123
 Tmp4 51                     IKHKKIIIITMILVLVLSLILSYGSIKYKSEQKMAQ-15 
 Tmp5 273   MKFIKKNKWALLASFFIPLILMVIVLAMTGIYWGSSRSILAGDAYHQYVAIHS-   
       -LYRNILHSGGSQGFLYTFTSGLGLNLYAFSAYYMGSFLMPFTFFFDV-   
                          -KSMPDALYLFTIIKFGLIGLSSFVSFKN-   
                              -MYQKLSNLTVLSISTAFALMSFLT-   
                          -SQLEITMWLDVFILLPLIIWGLHRLMDE-   
              -RKRWLYFVSLLILFIQNYYFGFMVAIFLVLYFLARMTYEKW-   
                   -SWTKVLDFVVSSTLAGIASLIMLLPMYLDLKSNNSD-16 
 Tmp6 118                   83-LPKHFFDIFKIACYIVIGYVLFFTIPYMVSPSSKL-   
 Tmp7 234         MMLKKEWQAILKHKFFIIVIIALALVPAIYNYIFLGSMWDPYGKLNDLP-185
a

Number of amino acids fused to ΔSPNuc. 

b

For Exp, Nlp, and Tmp polypeptides, classical signal peptides, lipoprotein signal peptides, and transmembrane domains, respectively, are presented. For the export signal sequences shown, charged amino acids are shown in italics, stretches of hydrophobic amino acids predicted to form a transmembrane domain are underlined, signal peptide cleavage regions (amino acids −3 to +1) are in boldface type, and predicted cleavage sites are indicated by arrows. Numbers to the left and/or right of the export signal indicate the length of polypeptide that is joined at that end in the fusion (the lack of a number signifies 0 amino acids). For Tmp5, the seven predicted transmembrane domains are presented. The start sites (the first amino acids [Met, Val, and Lev]) correspond to the most-N-terminal methionine, valine, or leucine and/or the first amino acid following a consensus ribosome-binding site. It should be noted that start sites are not confirmed, and alternative start sites are also possible. 

c

Isolated in experiments with a prescreening step in E. coli. Exp2 and Nlp1 were also isolated directly in L. lactis.