ID   LAN33_PROMM             Reviewed;          87 AA.
AC   Q7V7B7;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Lantipeptide prochlorosin 3.3 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
DE            Short=Lantipeptide Pcn3.3 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
DE   Flags: Precursor;
GN   Name=ProcA3.3 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
GN   OrderedLocusNames=PMT_0832 {ECO:0000312|EMBL:CAE21007.1};
OS   Prochlorococcus marinus (strain MIT 9313).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=74547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9313;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
RN   [2]
RP   PRELIMINARY LANTHIONINE CROSS-LINKS, DEHYDRATION AT THR-67, AND INDUCTION
RP   BY NITROGEN STARVATION.
RC   STRAIN=MIT 9313;
RX   PubMed=20479271; DOI=10.1073/pnas.0913677107;
RA   Li B., Sher D., Kelly L., Shi Y., Huang K., Knerr P.J., Joewono I.,
RA   Rusch D., Chisholm S.W., van der Donk W.A.;
RT   "Catalytic promiscuity in the biosynthesis of cyclic peptide secondary
RT   metabolites in planktonic marine cyanobacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:10430-10435(2010).
RN   [3]
RP   STRUCTURE BY NMR OF 65-87, DEHYDRATION AT THR-67, LANTHIONINE CROSS-LINKS,
RP   AND EXPRESSION IN E.COLI.
RC   STRAIN=MIT 9313;
RX   PubMed=22574919; DOI=10.1021/bi300255s;
RA   Tang W., van der Donk W.A.;
RT   "Structural characterization of four prochlorosins: a novel class of
RT   lantipeptides produced by planktonic marine cyanobacteria.";
RL   Biochemistry 51:4271-4279(2012).
CC   -!- FUNCTION: Lanthionine-containing peptide (lantipeptide) with unknown
CC       function (Probable). Does not show antibiotic activity against
CC       Lactococcus lactis 117 and Bacillus subtilis 6633 bacteria (By
CC       similarity). Organisms that produce this peptide live in oligotrophic
CC       environments at very dilute concentrations, suggesting this peptide is
CC       not secreted to influence other bacteria (Probable).
CC       {ECO:0000250|UniProtKB:Q7V8T1, ECO:0000305,
CC       ECO:0000305|PubMed:20479271, ECO:0000305|PubMed:22574919}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- INDUCTION: Down-regulated under nitrogen starvation.
CC       {ECO:0000269|PubMed:20479271}.
CC   -!- PTM: Cross-links are proved in vitro, when coepressed in E.coli with
CC       the ProcM lanthionine synthetase. {ECO:0000269|PubMed:22574919}.
CC   -!- PTM: The beta-methyllanthionine residues have a DL configuration (with
CC       2S,3S,6R stereochemistry). {ECO:0000269|PubMed:22574919}.
CC   -!- PTM: Maturation of prochlorosin involves the enzymatic conversion of
CC       Thr, and Ser into dehydrated AA and the formation of thioether bonds
CC       with cysteines. This is followed by membrane translocation and cleavage
CC       of the modified precursor. {ECO:0000250|UniProtKB:H2A7G5,
CC       ECO:0000305|PubMed:22574919}.
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DR   EMBL; BX548175; CAE21007.1; -; Genomic_DNA.
DR   RefSeq; WP_011130210.1; NC_005071.1.
DR   AlphaFoldDB; Q7V7B7; -.
DR   SMR; Q7V7B7; -.
DR   EnsemblBacteria; CAE21007; CAE21007; PMT_0832.
DR   KEGG; pmt:PMT_0832; -.
DR   HOGENOM; CLU_158613_2_0_3; -.
DR   OrthoDB; 1942394at2; -.
DR   Proteomes; UP000001423; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   InterPro; IPR022516; CHP03798_Ocin.
DR   InterPro; IPR012903; Nif11.
DR   Pfam; PF07862; Nif11; 1.
DR   TIGRFAMs; TIGR03798; ocin_TIGR03798; 1.
PE   1: Evidence at protein level;
KW   Reference proteome; Secreted; Thioether bond.
FT   PROPEP          1..64
FT                   /evidence="ECO:0000305|PubMed:20479271,
FT                   ECO:0000305|PubMed:22574919"
FT                   /id="PRO_0000450375"
FT   PEPTIDE         65..87
FT                   /note="Lantipeptide prochlorosin 3.3"
FT                   /evidence="ECO:0000305|PubMed:20479271,
FT                   ECO:0000305|PubMed:22574919"
FT                   /id="PRO_0000450376"
FT   MOD_RES         67
FT                   /note="2,3-didehydrobutyrine"
FT                   /evidence="ECO:0000269|PubMed:20479271,
FT                   ECO:0000269|PubMed:22574919"
FT   CROSSLNK        75..85
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:22574919,
FT                   ECO:0000305|PubMed:20479271"
FT   CROSSLNK        78..82
FT                   /note="Beta-methyllanthionine (Cys-Thr)"
FT                   /evidence="ECO:0000269|PubMed:22574919,
FT                   ECO:0000305|PubMed:20479271"
SQ   SEQUENCE   87 AA;  8902 MW;  631906F70B2D5021 CRC64;
     MSEEQLKAFI AKVQGDSSLQ EQLKAEGADV VAIAKAAGFT IKQQDLNAAA SELSDEELEA
     ASGGGDTGIQ AVLHTAGCYG GTKMCRA