PROT_BACS1
ID PROT_BACS1 Reviewed; 145 AA.
AC J9ZXD8;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 1.
DT 25-MAY-2022, entry version 16.
DE RecName: Full=Polytheonamide B {ECO:0000303|PubMed:22983711};
DE AltName: Full=Proteusin {ECO:0000303|PubMed:22983711};
DE Flags: Precursor;
GN Name=poyA {ECO:0000303|PubMed:22983711};
OS Bacterium symbiont subsp. Theonella swinhoei (strain pTSMAC1).
OC Bacteria.
OX NCBI_TaxID=1221190;
RN [1] {ECO:0000312|EMBL:AFS60639.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], EXPRESSION IN E.COLI, D-AMINO ACID AT
RP VAL-102; ALA-104; VAL-106; VAL-110; ASN-112; ASN-118; VAL-120; ASN-124;
RP ASN-126; VAL-128; ASN-130; ASN-132; ASN-134; ASN-136; SER-138; ASN-140;
RP ASN-142 AND THR-144, METHYLATION AT ILE-99; VAL-101; VAL-102; VAL-103;
RP VAL-105; VAL-106; VAL-110; ASN-112; THR-113; VAL-117; ASN-118; GLN-119;
RP ASN-124; ASN-126; VAL-127; ASN-130; ASN-132; ASN-134; ASN-136 AND MET-141,
RP AND HYDROXYLATION AT VAL-120; ASN-126; VAL-128 AND ASN-134.
RX PubMed=22983711; DOI=10.1126/science.1226121;
RA Freeman M.F., Gurgui C., Helf M.J., Morinaka B.I., Uria A.R., Oldham N.J.,
RA Sahl H.G., Matsunaga S., Piel J.;
RT "Metagenome mining reveals polytheonamides as posttranslationally modified
RT ribosomal peptides.";
RL Science 338:387-390(2012).
CC -!- FUNCTION: Antimicrobial peptide active against Gram-positive bacteria
CC (MIC=4->125 ug/ml) (PubMed:22983711). May act by forming transmembrane
CC ion channels, since the peptide rapidly depolarizes the bacterial
CC cytoplasmic membrane, simultaneously decreasing the membrane potential
CC and intracellular potassium contents (PubMed:22983711).
CC {ECO:0000269|PubMed:22983711}.
CC -!- PTM: Epimerization of most, and perhaps all, L- to D-amino acids is
CC catalyzed by PoyD, when PoyA and PoyD are coexpressed in E.coli.
CC {ECO:0000269|PubMed:22983711}.
CC -!- PTM: N-methylations are catalyzed by PoyE, when PoyA and PoyE are
CC coexpressed in E.coli. {ECO:0000269|PubMed:22983711}.
CC -!- PTM: To obtain 2-oxo-5,5-dimethylhexanoate, Thr-97 is firstly
CC dehydrated by PoyF (PubMed:22983711). The second step possibly
CC corresponds to methylation by PoyB/C, and the third step may be a
CC cleavage by PoyH/J (Probable). {ECO:0000269|PubMed:22983711,
CC ECO:0000305|PubMed:22983711}.
CC -!- MISCELLANEOUS: The name 'proteusin' is inspired by Proteus, a Greek
CC shape-shifting sea god. {ECO:0000305|PubMed:22983711}.
CC -!- MISCELLANEOUS: Compared to polytheonamide B, polytheonamide A has an
CC additional sulfoxide moiety at Met-141, which arises from spontaneous
CC oxidation during polytheonamide isolation.
CC {ECO:0000305|PubMed:22983711}.
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DR EMBL; JX456532; AFS60639.1; -; Genomic_DNA.
DR AlphaFoldDB; J9ZXD8; -.
DR TCDB; 1.D.24.1.1; the marine sponge polytheonamide b (ptb) family.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR Gene3D; 3.90.330.10; -; 1.
DR InterPro; IPR036648; CN_Hdrase_a/SCN_Hdrase_g_sf.
DR InterPro; IPR022513; TOMM_pelo.
DR SUPFAM; SSF56209; SSF56209; 1.
DR TIGRFAMs; TIGR03793; TOMM_pelo; 1.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; D-amino acid; Hydroxylation; Methylation.
FT PROPEP 1..96
FT /evidence="ECO:0000305|PubMed:22983711"
FT /id="PRO_0000450586"
FT CHAIN 97..145
FT /note="Polytheonamide B"
FT /evidence="ECO:0000305|PubMed:22983711"
FT /id="PRO_0000450587"
FT MOD_RES 97
FT /note="2-oxo-5,5-dimethylhexanoate"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 99
FT /note="3-methylisoleucine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 101
FT /note="3-methylvaline"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 102
FT /note="3-methyl-D-valine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 103
FT /note="3-methylvaline"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 104
FT /note="D-alanine (Ala)"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 105
FT /note="3-methylvaline"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 106
FT /note="3-methyl-D-valine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 110
FT /note="3-methyl-D-valine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 112
FT /note="N4-methyl-D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 113
FT /note="3-hydroxyvaline (Thr)"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 117
FT /note="3-methylvaline"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 118
FT /note="N4-methyl-D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 119
FT /note="(3S)-3-methylglutamine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 120
FT /note="3-hydroxy-D-valine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 124
FT /note="N4-methyl-D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 126
FT /note="(3R)-N4-methyl-3-hydroxy-D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 127
FT /note="3-methylvaline"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 128
FT /note="3-hydroxy-D-valine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 130
FT /note="N4-methyl-D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 132
FT /note="N4-methyl-D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 134
FT /note="(3R)-N4-methyl-3-hydroxy-D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 136
FT /note="N4-methyl-D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 138
FT /note="D-serine (Ser)"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 140
FT /note="D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 141
FT /note="3,3-dimethylmethionine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 142
FT /note="D-asparagine"
FT /evidence="ECO:0000269|PubMed:22983711"
FT MOD_RES 144
FT /note="D-threonine"
FT /evidence="ECO:0000269|PubMed:22983711"
SQ SEQUENCE 145 AA; 15425 MW; A01FD18DAF5944EE CRC64;
MADSDNTPTS RKDFETAIIA KAWKDPEYLR RLRSNPREVL QEELEALHPG AQLPDDLGIS
IHEEDENHVH LVMPRHPQNV SDQTLTDDDL DQAAGGTGIG VVVAVVAGAV ANTGAGVNQV
AGGNINVVGN INVNANVSVN MNQTT
