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LANA2_LACLL
ID   LANA2_LACLL             Reviewed;          65 AA.
AC   O87237;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 57.
DE   RecName: Full=Lantibiotic lacticin 3147 A2;
DE   Flags: Precursor;
GN   Name=ltnA2 {ECO:0000303|PubMed:10608807};
GN   Synonyms=ltnB {ECO:0000312|EMBL:AAF32257.1}; ORFNames=ORF00036;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG   Plasmid pMRC01 {ECO:0000312|EMBL:AAC56054.1}, and
OG   Plasmid pBAC105 {ECO:0000312|EMBL:AAF32257.1}.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1] {ECO:0000312|EMBL:AAC56054.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DPC3147 {ECO:0000312|EMBL:AAC56054.1}; PLASMID=pMRC01;
RX   PubMed=9767571; DOI=10.1046/j.1365-2958.1998.00988.x;
RA   Dougherty B.A., Hill C., Weidman J.F., Richardson D.R., Venter J.C.,
RA   Ross R.P.;
RT   "Sequence and analysis of the 60 kb conjugative, bacteriocin-producing
RT   plasmid pMRC01 from Lactococcus lactis DPC3147.";
RL   Mol. Microbiol. 29:1029-1038(1998).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:AAF32257.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 51-57, FUNCTION,
RP   SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=IFPL105 {ECO:0000312|EMBL:AAF32257.1}; PLASMID=pBAC105;
RX   PubMed=10971756; DOI=10.1046/j.1365-2672.2000.01103.x;
RA   Martinez-Cuesta M.C., Buist G., Kok J., Hauge H.H., Nissen-Meyer J.,
RA   Pelaez C., Requena T.;
RT   "Biological and molecular characterization of a two-peptide lantibiotic
RT   produced by Lactococcus lactis IFPL105.";
RL   J. Appl. Microbiol. 89:249-260(2000).
RN   [3] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 37-65, MASS SPECTROMETRY, THIOETHER BONDS, AND
RP   DEHYDRATION AT THR-38; THR-41; SER-45 AND SER-48.
RC   STRAIN=DPC3147 {ECO:0000269|PubMed:15023056};
RX   PubMed=15023056; DOI=10.1021/bi0362065;
RA   Martin N.I., Sprules T., Carpenter M.R., Cotter P.D., Hill C., Ross R.P.,
RA   Vederas J.C.;
RT   "Structural characterization of lacticin 3147, a two-peptide lantibiotic
RT   with synergistic activity.";
RL   Biochemistry 43:3049-3056(2004).
RN   [4] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, AND MASS SPECTROMETRY.
RC   STRAIN=DPC3147 {ECO:0000269|PubMed:10608807};
RX   PubMed=10608807; DOI=10.1074/jbc.274.53.37544;
RA   Ryan M.P., Jack R.W., Josten M., Sahl H.-G., Jung G., Ross R.P., Hill C.;
RT   "Extensive post-translational modification, including serine to D-alanine
RT   conversion, in the two-component lantibiotic, lacticin 3147.";
RL   J. Biol. Chem. 274:37544-37550(1999).
CC   -!- FUNCTION: Lanthionine-containing peptide antibiotic (lantibiotic)
CC       active on Gram-positive bacteria. The bactericidal activity of
CC       lantibiotics is based on depolarization of energized bacterial
CC       cytoplasmic membranes, initiated by the formation of aqueous
CC       transmembrane pores. When present individually lacticin 3147 A2
CC       exhibits weak activity towards L.lactis strain AM2 and L.lactis strain
CC       HP, and no activity towards L.lactis strain IFPL359, but when combined
CC       with lacticin 3147 A1 it displays strong activity towards all three
CC       strains. {ECO:0000269|PubMed:10608807, ECO:0000269|PubMed:10971756}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10608807,
CC       ECO:0000269|PubMed:10971756}.
CC   -!- PTM: Maturation of lantibiotics involves the enzymatic conversion of
CC       Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC       with cysteine. This is followed by membrane translocation and cleavage
CC       of the modified precursor. {ECO:0000269|PubMed:15023056}.
CC   -!- PTM: It is not established whether the 2,3-didehydrobutyrines are the
CC       E- or Z-isomers (PubMed:15023056 and PubMed:10608807). In the NMR model
CC       they were assumed to be the Z-isomer.
CC   -!- MASS SPECTROMETRY: Mass=2848; Method=Plasma desorption;
CC       Evidence={ECO:0000269|PubMed:10971756};
CC   -!- MASS SPECTROMETRY: Mass=2847.40; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15023056};
CC   -!- MASS SPECTROMETRY: Mass=2847.47; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10608807};
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DR   EMBL; AE001272; AAC56054.1; -; Genomic_DNA.
DR   EMBL; AF167432; AAF32257.1; -; Genomic_DNA.
DR   PIR; T43107; T43107.
DR   RefSeq; NP_047320.1; NC_001949.1.
DR   AlphaFoldDB; O87237; -.
DR   TCDB; 1.C.21.2.4; the lacticin 481 (lacticin 481) family.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Lantibiotic; Plasmid; Secreted; Thioether bond.
FT   PROPEP          1..36
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT                   /id="PRO_0000042851"
FT   PEPTIDE         37..65
FT                   /note="Lantibiotic lacticin 3147 A2"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT                   /id="PRO_0000042852"
FT   MOD_RES         37
FT                   /note="2-oxobutanoic acid"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   MOD_RES         38
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   MOD_RES         41
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   MOD_RES         45
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   MOD_RES         48
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   CROSSLNK        52..56
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   CROSSLNK        58..61
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   CROSSLNK        62..65
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
SQ   SEQUENCE   65 AA;  7080 MW;  DD063A6B5DCE5F82 CRC64;
     MKEKNMKKND TIELQLGKYL EDDMIELAEG DESHGGTTPA TPAISILSAY ISTNTCPTTK
     CTRAC
 
 
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