ID   SAV2_STRVL              Reviewed;         183 AA.
AC   Q53533;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Streptavidin-V2;
DE            Short=SA V2;
DE   Flags: Precursor;
OS   Streptomyces violaceus (Streptomyces venezuelae).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1936;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7632734; DOI=10.1016/0167-4781(95)00077-t;
RA   Bayer E.A., Kulik T., Adar R., Wilchek M.;
RT   "Close similarity among streptavidin-like, biotin-binding proteins from
RT   Streptomyces.";
RL   Biochim. Biophys. Acta 1263:60-66(1995).
CC   -!- FUNCTION: The biological function of streptavidin is not known. Forms a
CC       strong non-covalent specific complex with biotin (one molecule of
CC       biotin per subunit of streptavidin).
CC   -!- SUBUNIT: Homotetramer. {ECO:0000255|PROSITE-ProRule:PRU00656}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the avidin/streptavidin family. {ECO:0000305}.
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DR   EMBL; S78782; AAB35016.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53533; -.
DR   SMR; Q53533; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR   Gene3D; 2.40.128.30; -; 1.
DR   InterPro; IPR005469; Avidin.
DR   InterPro; IPR017889; Avidin-like_CS.
DR   InterPro; IPR036896; Avidin-like_sf.
DR   InterPro; IPR005468; Avidin/str.
DR   Pfam; PF01382; Avidin; 1.
DR   PRINTS; PR00709; AVIDIN.
DR   SUPFAM; SSF50876; SSF50876; 1.
DR   PROSITE; PS00577; AVIDIN_1; 1.
DR   PROSITE; PS51326; AVIDIN_2; 1.
PE   3: Inferred from homology;
KW   Biotin; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000250"
FT   CHAIN           25..183
FT                   /note="Streptavidin-V2"
FT                   /id="PRO_0000002731"
FT   DOMAIN          37..159
FT                   /note="Avidin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00656"
FT   MOTIF           83..85
FT                   /note="Cell attachment site; atypical"
FT   BINDING         67
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
FT   BINDING         116
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
FT   BINDING         144
FT                   /ligand="biotin"
FT                   /ligand_id="ChEBI:CHEBI:57586"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   183 AA;  18833 MW;  FEAFFFFDFEA4ECCA CRC64;
     MRKIVVAAIA VSLTTVGITA SASADPSKDS KAQAAVAEAG ITGTWYNQLG STFIVTANAD
     GSLTGTYESA VGNAESRYVL TGRYDSAPAT DGSGTALGWT VAWKNNYRNA HSATTWSGQY
     VAGSEARINT QWLLTSGTTA ANAWKSTLVG HDTFTKVKPS AASIDAAKKA GVNNGNPLDA
     VQQ