ID   WAPA_OXYMI              Reviewed;          50 AA.
AC   P83952;
DT   21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Omwaprin-a {ECO:0000250|UniProtKB:B5G6G7};
DE            Short=Omwaprin {ECO:0000303|PubMed:17044815, ECO:0000303|PubMed:20669184};
DE   AltName: Full=Oxywaprin-a {ECO:0000250|UniProtKB:B5L5M9};
OS   Oxyuranus microlepidotus (Inland taipan) (Diemenia microlepidota).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Oxyuranus.
OX   NCBI_TaxID=111177;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, MASS SPECTROMETRY, AND
RP   DISULFIDE BONDS.
RC   TISSUE=Venom;
RX   PubMed=17044815; DOI=10.1042/bj20060318;
RA   Nair D.G., Fry B.G., Alewood P.F., Kumar P.P., Kini R.M.;
RT   "Antimicrobial activity of omwaprin, a new member of the waprin family of
RT   snake venom proteins.";
RL   Biochem. J. 402:93-104(2007).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF RACEMIC MIXTURE OF BOTH
RP   L-OMWAPRIN AND D-OMWAPRIN, DISULFIDE BOND, AND SYNTHESIS OF L-OMWAPRIN AND
RP   D-OMWAPRIN.
RX   PubMed=20669184; DOI=10.1002/pro.468;
RA   Banigan J.R., Mandal K., Sawaya M.R., Thammavongsa V., Hendrickx A.P.,
RA   Schneewind O., Yeates T.O., Kent S.B.;
RT   "Determination of the X-ray structure of the snake venom protein omwaprin
RT   by total chemical synthesis and racemic protein crystallography.";
RL   Protein Sci. 19:1840-1849(2010).
CC   -!- FUNCTION: Damages membranes of susceptible bacteria (PubMed:17044815).
CC       Has antibacterial activity against the Gram-positive bacteria
CC       B.megaterium and S.warneri (PubMed:17044815, PubMed:20669184). After a
CC       45-minute treatment with this protein, B.megaterium have no visible
CC       pili and are smooth (PubMed:20669184). Has no antibacterial activity
CC       against the Gram-positive bacteria B.thuringiensis, S.aureus,
CC       S.clavuligerus and B. anthracis, or the Gram-negative bacteria E.coli
CC       and A.tumefaciens (PubMed:17044815, PubMed:20669184). Has no hemolytic
CC       activity (PubMed:17044815). Does not inhibit the proteinases elastase
CC       and cathepsin G (PubMed:17044815). Is not toxic to mice
CC       (PubMed:17044815). {ECO:0000269|PubMed:17044815}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:17044815}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:17044815}.
CC   -!- MASS SPECTROMETRY: Mass=5602; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:17044815};
CC   -!- MISCELLANEOUS: A D-omwaprin has been synthesized to permit
CC       cristallization by using a racemic mixture containing equal amounts of
CC       L- and D-omwaprin. This D-omwaprin provokes B.megaterium lysis (after
CC       45 minutes of treatment), but fails to inhibit growth of B.anthracis.
CC       {ECO:0000269|PubMed:20669184}.
CC   -!- SIMILARITY: Belongs to the snake waprin family. {ECO:0000305}.
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DR   PDB; 3NGG; X-ray; 1.33 A; A/B=1-50.
DR   PDBsum; 3NGG; -.
DR   AlphaFoldDB; P83952; -.
DR   SMR; P83952; -.
DR   PRIDE; P83952; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030414; F:peptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.75.10; -; 1.
DR   InterPro; IPR036645; Elafin-like_sf.
DR   InterPro; IPR008197; WAP_dom.
DR   Pfam; PF00095; WAP; 1.
DR   PRINTS; PR00003; 4DISULPHCORE.
DR   SMART; SM00217; WAP; 1.
DR   SUPFAM; SSF57256; SSF57256; 1.
DR   PROSITE; PS51390; WAP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic; Antimicrobial; Direct protein sequencing;
KW   Disulfide bond; Secreted.
FT   CHAIN           1..50
FT                   /note="Omwaprin-a"
FT                   /evidence="ECO:0000269|PubMed:17044815"
FT                   /id="PRO_0000188989"
FT   DOMAIN          3..47
FT                   /note="WAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00722"
FT   DISULFID        10..35
FT                   /evidence="ECO:0000269|PubMed:17044815,
FT                   ECO:0000269|PubMed:20669184, ECO:0000312|PDB:3NGG"
FT   DISULFID        18..39
FT                   /evidence="ECO:0000269|PubMed:17044815,
FT                   ECO:0000269|PubMed:20669184, ECO:0000312|PDB:3NGG"
FT   DISULFID        22..34
FT                   /evidence="ECO:0000269|PubMed:17044815,
FT                   ECO:0000269|PubMed:20669184, ECO:0000312|PDB:3NGG"
FT   DISULFID        28..43
FT                   /evidence="ECO:0000269|PubMed:17044815,
FT                   ECO:0000269|PubMed:20669184, ECO:0000312|PDB:3NGG"
FT   STRAND          7..9
FT                   /evidence="ECO:0007829|PDB:3NGG"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:3NGG"
FT   STRAND          33..36
FT                   /evidence="ECO:0007829|PDB:3NGG"
FT   STRAND          41..44
FT                   /evidence="ECO:0007829|PDB:3NGG"
SQ   SEQUENCE   50 AA;  5611 MW;  18654615BAE58FC6 CRC64;
     KDRPKKPGLC PPRPQKPCVK ECKNDDSCPG QQKCCNYGCK DECRDPIFVG