LAN17_PROMM
ID LAN17_PROMM Reviewed; 90 AA.
AC Q7TV59;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Lantipeptide prochlorosin 1.7 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
DE Short=Lantipeptide Pcn1.7 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
DE Flags: Precursor;
GN Name=ProcA1.7 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
GN OrderedLocusNames=PMT_0239 {ECO:0000312|EMBL:CAE20414.1};
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, DEHYDRATION AT THR-69 AND THR-73, AND INDUCTION BY
RP 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 69-90, DEHYDRATION AT THR-69 AND THR-73, LANTHIONINE
RP CROSS-LINKS, 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 lanthionine residue has a DL configuration (with 2S,6R
CC stereochemistry), whereas the beta-methyllanthionine residues have a DL
CC configuration (with 2S,3S,6R stereochemistry).
CC {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=CAE20414.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305|PubMed:22574919};
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DR EMBL; BX548175; CAE20414.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041384871.1; NC_005071.1.
DR AlphaFoldDB; Q7TV59; -.
DR SMR; Q7TV59; -.
DR STRING; 74547.PMT_0239; -.
DR EnsemblBacteria; CAE20414; CAE20414; PMT_0239.
DR KEGG; pmt:PMT_0239; -.
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 Reference proteome; Secreted; Thioether bond.
FT PROPEP 1..68
FT /evidence="ECO:0000305|PubMed:20479271,
FT ECO:0000305|PubMed:22574919"
FT /id="PRO_0000450373"
FT PEPTIDE 69..90
FT /note="Lantipeptide prochlorosin 1.7"
FT /evidence="ECO:0000305|PubMed:20479271,
FT ECO:0000305|PubMed:22574919"
FT /id="PRO_0000450374"
FT MOD_RES 69
FT /note="2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20479271,
FT ECO:0000269|PubMed:22574919"
FT MOD_RES 73
FT /note="2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:20479271,
FT ECO:0000269|PubMed:22574919"
FT CROSSLNK 76..79
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:22574919,
FT ECO:0000305|PubMed:20479271"
FT CROSSLNK 78..82
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:22574919,
FT ECO:0000305|PubMed:20479271"
FT CROSSLNK 81..90
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:22574919,
FT ECO:0000305|PubMed:20479271"
SQ SEQUENCE 90 AA; 9342 MW; 87FB425CE05AEC2B CRC64;
MSEEQLKAFI AKVQADTSLQ EQLKVEGADV VAIAKASGFA ITTEDLKAHQ ANSQKNLSDA
ELEGVAGGTI GGTIVSITCE TCDLLVGKMC
