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LANA1_LACLL
ID   LANA1_LACLL             Reviewed;          59 AA.
AC   O87236;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 56.
DE   RecName: Full=Lantibiotic lacticin 3147 A1;
DE   Flags: Precursor;
GN   Name=ltnA1 {ECO:0000303|PubMed:10608807};
GN   Synonyms=ltnA {ECO:0000312|EMBL:AAF32256.1}; ORFNames=ORF00035;
OS   Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG   Plasmid pMRC01 {ECO:0000312|EMBL:AAC56053.1}, and
OG   Plasmid pBAC105 {ECO:0000312|EMBL:AAF32256.1}.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=1360;
RN   [1] {ECO:0000312|EMBL:AAC56053.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DPC3147 {ECO:0000312|EMBL:AAC56053.1}; 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:AAF32256.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP   SPECTROMETRY.
RC   STRAIN=IFPL105 {ECO:0000312|EMBL:AAF32256.1}; 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 30-59, MASS SPECTROMETRY, THIOETHER BONDS, AND
RP   DEHYDRATION AT THR-32; THR-34 AND SER-36.
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   PROTEIN SEQUENCE OF 30-47, FUNCTION, SUBCELLULAR LOCATION, AND MASS
RP   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 A1
CC       exhibits strong activity towards L.lactis strain AM2, weak activity
CC       towards L.lactis strain HP and no activity towards L.lactis strain
CC       IFPL359, but when combined with lacticin 3147 A2 it displays strong
CC       activity towards all three strains. {ECO:0000269|PubMed:10608807,
CC       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=3322; Method=Plasma desorption;
CC       Evidence={ECO:0000269|PubMed:10971756};
CC   -!- MASS SPECTROMETRY: Mass=3306.69; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15023056};
CC   -!- MASS SPECTROMETRY: Mass=3322.34; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:10608807};
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DR   EMBL; AE001272; AAC56053.1; -; Genomic_DNA.
DR   EMBL; AF167432; AAF32256.1; -; Genomic_DNA.
DR   PIR; T43106; T43106.
DR   RefSeq; NP_047319.1; NC_001949.1.
DR   AlphaFoldDB; O87236; -.
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.
DR   InterPro; IPR029243; Lantibiotic_alpha.
DR   Pfam; PF14867; Lantibiotic_a; 1.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW   Lantibiotic; Plasmid; Secreted; Thioether bond.
FT   PROPEP          1..29
FT                   /evidence="ECO:0000269|PubMed:10608807,
FT                   ECO:0000269|PubMed:15023056"
FT                   /id="PRO_0000042849"
FT   PEPTIDE         30..59
FT                   /note="Lantibiotic lacticin 3147 A1"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT                   /id="PRO_0000042850"
FT   MOD_RES         32
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   MOD_RES         34
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   MOD_RES         36
FT                   /note="2,3-didehydroalanine (Ser)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   CROSSLNK        30..31
FT                   /note="Lanthionine (Cys-Ser)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   CROSSLNK        38..48
FT                   /note="Lanthionine (Ser-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   CROSSLNK        49..54
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
FT   CROSSLNK        51..58
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:15023056"
SQ   SEQUENCE   59 AA;  6798 MW;  850B313769976D42 CRC64;
     MNKNEIETQP VTWLEEVSDQ NFDEDVFGAC STNTFSLSDY WGNNGAWCTL THECMAWCK
 
 
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