LANP_STAEP
ID LANP_STAEP Reviewed; 60 AA.
AC P19578;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Lantibiotic Pep5;
DE Flags: Precursor;
GN Name=pepA;
OS Staphylococcus epidermidis.
OG Plasmid.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=5;
RX PubMed=2764678; DOI=10.1007/bf00447005;
RA Kaletta C., Entian K.-D., Kellner R., Jung G., Reis M., Sahl H.-G.;
RT "Pep5, a new lantibiotic: structural gene isolation and prepeptide
RT sequence.";
RL Arch. Microbiol. 152:16-19(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=5;
RX PubMed=7556197; DOI=10.1111/j.1432-1033.1995.tb20834.x;
RA Meyer C., Bierbaum G., Heidrich C., Reis M., Suling J., Iglesias-Wind M.,
RA Kempter C., Molitor E., Sahl H.-G.;
RT "Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and
RT functional analysis of PepP and PepC. Evidence for a role of PepC in
RT thioether formation.";
RL Eur. J. Biochem. 232:478-489(1995).
RN [3]
RP PROTEIN SEQUENCE OF 1-26, DEHYDRATION AT THR-42 AND THR-46, OXOBUTANOIC
RP ACID FORMATION AT THR-27, AND LANTHIONINE CROSS-LINKS.
RX PubMed=2253617; DOI=10.1111/j.1432-1033.1990.tb19446.x;
RA Weil H.-P., Beck-Sickinger A.G., Metzger J., Stevanovic S., Jung G.,
RA Josten M.;
RT "Biosynthesis of the lantibiotic Pep5. Isolation and characterization of a
RT prepeptide containing dehydroamino acids.";
RL Eur. J. Biochem. 194:217-223(1990).
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.
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.
CC -!- PTM: After proteolysis of the propeptide, the N-terminal 2,3-
CC didehydrobutyrine hydrolyzes to 2-oxobutanoic acid, possibly
CC spontaneously.
CC -!- SIMILARITY: Belongs to the type A lantibiotic family. {ECO:0000305}.
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DR EMBL; L23967; AAA65876.1; -; Genomic_DNA.
DR EMBL; Z49865; CAA90023.1; -; Genomic_DNA.
DR PIR; JL0100; LPSE5.
DR RefSeq; WP_029376348.1; NZ_SCHF01000025.1.
DR AlphaFoldDB; P19578; -.
DR TCDB; 1.C.20.1.3; the nisin (nisin) family.
DR GO; GO:0005102; F:signaling receptor binding; IEA:UniProtKB-KW.
DR GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR InterPro; IPR012519; Lantibiotic_typ-A_Pep5.
DR Pfam; PF08130; Antimicrobial18; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Bacteriocin; Direct protein sequencing;
KW Lantibiotic; Plasmid; Thioether bond.
FT PROPEP 1..26
FT /evidence="ECO:0000269|PubMed:2253617"
FT /id="PRO_0000017140"
FT PEPTIDE 27..60
FT /note="Lantibiotic Pep5"
FT /id="PRO_0000017141"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="2-oxobutanoic acid"
FT /evidence="ECO:0000305|PubMed:2253617"
FT MOD_RES 42
FT /note="2,3-didehydrobutyrine"
FT /evidence="ECO:0000305|PubMed:2253617"
FT MOD_RES 46
FT /note="2,3-didehydrobutyrine"
FT /evidence="ECO:0000305|PubMed:2253617"
FT CROSSLNK 35..39
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000305|PubMed:2253617"
FT CROSSLNK 50..53
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000305|PubMed:2253617"
FT CROSSLNK 52..59
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000305|PubMed:2253617"
SQ SEQUENCE 60 AA; 6685 MW; 44D0512A01782532 CRC64;
MKNNKNLFDL EIKKETSQNT DELEPQTAGP AIRASVKQCQ KTLKATRLFT VSCKGKNGCK
