LAN43_PROMM
ID LAN43_PROMM Reviewed; 77 AA.
AC Q7V735;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=Lantipeptide prochlorosin 4.3 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
DE Short=Lantipeptide Pcn4.3 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
DE Flags: Precursor;
GN Name=ProcA4.3 {ECO:0000303|PubMed:20479271, ECO:0000303|PubMed:22574919};
GN OrderedLocusNames=PMT_0926 {ECO:0000312|EMBL:CAE21101.1};
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-65, 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 65-77, DEHYDRATION AT THR-65, 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 lanthionine residue has both a DL configuration (with 2S,6R
CC stereochemistry) and a LL configuration (with 2R,6R stereochemistry)
CC (PubMed:22574919). DL and LL diastomers have a 4:1 ratio
CC (PubMed:22574919). It is unknown whether nonenzymatic cyclization
CC occur, but authors favor a model in which ProcM does generate all
CC thioether cross-links (Probable). The beta-methyllanthionine residue
CC has a DL configuration (with 2S,3S,6R stereochemistry)
CC (PubMed:22574919). {ECO:0000269|PubMed:22574919,
CC ECO:0000305|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; CAE21101.1; -; Genomic_DNA.
DR RefSeq; WP_011130304.1; NC_005071.1.
DR AlphaFoldDB; Q7V735; -.
DR SMR; Q7V735; -.
DR EnsemblBacteria; CAE21101; CAE21101; PMT_0926.
DR KEGG; pmt:PMT_0926; -.
DR eggNOG; ENOG5034BZY; Bacteria.
DR HOGENOM; CLU_158613_2_0_3; -.
DR OMA; DTSMFCY; -.
DR OrthoDB; 2187917at2; -.
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_0000450377"
FT PEPTIDE 65..77
FT /note="Lantipeptide prochlorosin 4.3"
FT /evidence="ECO:0000305|PubMed:20479271,
FT ECO:0000305|PubMed:22574919"
FT /id="PRO_0000450378"
FT MOD_RES 65
FT /note="2,3-didehydrobutyrine"
FT /evidence="ECO:0000269|PubMed:22574919,
FT ECO:0000305|PubMed:20479271"
FT CROSSLNK 67..70
FT /note="Lanthionine (Ser-Cys)"
FT /evidence="ECO:0000269|PubMed:22574919,
FT ECO:0000305|PubMed:20479271"
FT CROSSLNK 72..76
FT /note="Beta-methyllanthionine (Thr-Cys)"
FT /evidence="ECO:0000269|PubMed:22574919,
FT ECO:0000305|PubMed:20479271"
SQ SEQUENCE 77 AA; 8100 MW; 763CF6554E7C6C56 CRC64;
MSEEQLKAFI AKVQADTSLQ EQLKAEGADV VAIAKAAGFT ITTEDLNSHR QNLTDDELEG
VAGGTASGGC DTSMFCY
