SILU_RHIPU
ID SILU_RHIPU Reviewed; 30 AA.
AC P02885;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 11-DEC-2019, entry version 46.
DE RecName: Full=Sillucin;
OS Rhizomucor pusillus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Lichtheimiaceae; Rhizomucor.
OX NCBI_TaxID=4840;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=761621; DOI=10.1016/0014-5793(79)80057-5;
RA Bradley W.A., Somkuti G.A.;
RT "The primary structure of sillucin and antimicrobial peptide from Mucor
RT pusillus.";
RL FEBS Lett. 97:81-83(1979).
RN [2]
RP DISULFIDE BONDS.
RX PubMed=11294620; DOI=10.1021/bi002229x;
RA Qi J., Wu J., Somkuti G.A., Watson J.T.;
RT "Determination of the disulfide structure of sillucin, a highly knotted,
RT cysteine-rich peptide, by cyanylation/cleavage mass mapping.";
RL Biochemistry 40:4531-4538(2001).
CC -!- FUNCTION: Sillucin is an antimicrobial agent produced by the
CC thermophilic fungus Rhizomucor pusillus in liquid culture; it is
CC effective against Gram-positive bacteria at the level of RNA
CC metabolism.
CC -!- SUBCELLULAR LOCATION: Secreted.
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DR PIR; A03380; SNUMP.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
PE 1: Evidence at protein level;
KW Antibiotic; Antimicrobial; Direct protein sequencing; Disulfide bond;
KW Secreted.
FT PEPTIDE 1..30
FT /note="Sillucin"
FT /id="PRO_0000044219"
FT DISULFID 2..7
FT /evidence="ECO:0000269|PubMed:11294620"
FT DISULFID 12..24
FT /evidence="ECO:0000269|PubMed:11294620"
FT DISULFID 13..30
FT /evidence="ECO:0000269|PubMed:11294620"
FT DISULFID 14..21
FT /evidence="ECO:0000269|PubMed:11294620"
SQ SEQUENCE 30 AA; 3209 MW; F0F0F067FF2BEC3E CRC64;
ACLPNSCVSK GCCCGBSGYW CRQCGIKYTC