ID   LAN11_PROMM             Reviewed;          81 AA.
AC   Q7V8T1;
DT   17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT   17-JUN-2020, sequence version 2.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Lantipeptide prochlorosin 1.1 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
DE            Short=Lantipeptide Pcn1.1 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
DE   Flags: Precursor;
GN   Name=ProcA1.1 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
GN   OrderedLocusNames=PMT_0247 {ECO:0000312|EMBL:CAE20422.1};
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   LANTHIONINE CROSS-LINKS, INDUCTION BY NITROGEN STARVATION, AND FUNCTION.
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 66-81, EXPRESSION IN E.COLI, AND LANTHIONINE
RP   CROSS-LINKS.
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
CC       (PubMed:20479271). Organisms that produce this peptide live in
CC       oligotrophic environments at very dilute concentrations, suggesting
CC       this peptide is not secreted to influence other bacteria (Probable).
CC       {ECO:0000269|PubMed:20479271, ECO:0000305, ECO:0000305|PubMed:20479271,
CC       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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE20422.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:22574919};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX548175; CAE20422.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_052646211.1; NC_005071.1.
DR   PDB; 6VHJ; NMR; -; A=66-81.
DR   PDBsum; 6VHJ; -.
DR   AlphaFoldDB; Q7V8T1; -.
DR   SMR; Q7V8T1; -.
DR   STRING; 74547.PMT_0247; -.
DR   EnsemblBacteria; CAE20422; CAE20422; PMT_0247.
DR   KEGG; pmt:PMT_0247; -.
DR   HOGENOM; CLU_158613_2_0_3; -.
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   3D-structure; Reference proteome; Secreted; Thioether bond.
FT   PROPEP          1..65
FT                   /evidence="ECO:0000305|PubMed:20479271,
FT                   ECO:0000305|PubMed:22574919"
FT                   /id="PRO_0000450371"
FT   PEPTIDE         66..81
FT                   /note="Lantipeptide prochlorosin 1.1"
FT                   /evidence="ECO:0000305|PubMed:20479271,
FT                   ECO:0000305|PubMed:22574919"
FT                   /id="PRO_0000450372"
FT   CROSSLNK        68..72
FT                   /note="Beta-methyllanthionine (Cys-Thr)"
FT                   /evidence="ECO:0000269|PubMed:22574919,
FT                   ECO:0000305|PubMed:20479271"
FT   CROSSLNK        77..81
FT                   /note="Beta-methyllanthionine (Thr-Cys)"
FT                   /evidence="ECO:0000269|PubMed:22574919,
FT                   ECO:0000305|PubMed:20479271"
SQ   SEQUENCE   81 AA;  8708 MW;  FED550F046B33CBA CRC64;
     MSEEQLKAFI AKVQADTSLQ EQLKAEGADV VAIAKAAGFS ITTEDLEKEH RQTLSDDDLE
     GVAGGFFCVQ GTANRFTINV C