HOAVI_HOEPD
ID HOAVI_HOEPD Reviewed; 164 AA.
AC A9D857;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 47.
DE RecName: Full=Hoefavidin {ECO:0000303|PubMed:26126731};
DE Flags: Precursor;
GN ORFNames=HPDFL43_17171 {ECO:0000312|EMBL:EDQ33228.1};
OS Hoeflea phototrophica (strain DSM 17068 / NCIMB 14078 / DFL-43).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Hoeflea.
OX NCBI_TaxID=411684;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17068 / NCIMB 14078 / DFL-43 {ECO:0000312|EMBL:EDQ33228.1};
RX PubMed=24019991; DOI=10.4056/sigs.3486982;
RA Fiebig A., Pradella S., Petersen J., Michael V., Paeuker O., Rohde M.,
RA Goeker M., Klenk H.P., Wagner-Doebler I.;
RT "Genome of the marine alphaproteobacterium Hoeflea phototrophica type
RT strain (DFL-43(T)).";
RL Stand. Genomic Sci. 7:440-448(2013).
RN [2]
RP SUBUNIT.
RC STRAIN=DSM 17068 / NCIMB 14078 / DFL-43;
RX PubMed=29720692; DOI=10.1038/s41598-018-25246-6;
RA Amartely H., Avraham O., Friedler A., Livnah O., Lebendiker M.;
RT "Coupling multi angle light scattering to ion exchange chromatography (IEX-
RT MALS) for protein characterization.";
RL Sci. Rep. 8:6907-6907(2018).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.17 ANGSTROMS) OF APOPROTEIN AND IN COMPLEXES WITH
RP BIOTIN AND C-TERMINAL DERIVED PEPTIDES, FUNCTION, DISULFIDE BOND, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND BIOTECHNOLOGY.
RC STRAIN=DSM 17068 / NCIMB 14078 / DFL-43;
RX PubMed=26126731; DOI=10.1016/j.jsb.2015.06.020;
RA Avraham O., Meir A., Fish A., Bayer E.A., Livnah O.;
RT "Hoefavidin: A dimeric bacterial avidin with a C-terminal binding tail.";
RL J. Struct. Biol. 191:139-148(2015).
CC -!- FUNCTION: The exact role played by hoefavidin in the host organism is
CC still obscure. Forms a strong non-covalent complex with biotin and 2-
CC iminobiotin. {ECO:0000269|PubMed:26126731}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Is hyperthermostable. Displays a Tm value of 84.9 degrees Celsius,
CC which increases to 96.2 degrees Celsius upon biotin binding.
CC {ECO:0000269|PubMed:26126731};
CC -!- SUBUNIT: Homodimer (PubMed:26126731). A later study shows that
CC hoefavidin can exist in different homooligomeric states: dimer,
CC tetramer, hexamer and octamer (PubMed:29720692). The X-ray structure of
CC the intact hoefavidin reveals unique crystal packing generated by an
CC octameric cylindrical structure wherein the C-terminal segments of each
CC monomer are introduced into the entrance of the biotin-binding site of
CC an adjacent non-canonical monomer (PubMed:26126731).
CC {ECO:0000269|PubMed:26126731, ECO:0000269|PubMed:29720692}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- BIOTECHNOLOGY: The specific properties of hoefavidin make it an
CC attractive target for novel biotechnological applications, including
CC drug delivery, nanotechnology, and molecular labeling.
CC {ECO:0000305|PubMed:26126731}.
CC -!- SIMILARITY: Belongs to the avidin/streptavidin family. {ECO:0000305}.
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DR EMBL; ABIA03000004; EDQ33228.1; -; Genomic_DNA.
DR RefSeq; WP_007199185.1; NZ_CM002917.1.
DR PDB; 4Z27; X-ray; 1.34 A; A/B=21-154.
DR PDB; 4Z28; X-ray; 1.66 A; A/B=21-154.
DR PDB; 4Z2O; X-ray; 1.17 A; A=21-154, P=153-164.
DR PDB; 4Z2P; X-ray; 1.60 A; A/B=21-154, C/P=153-164.
DR PDB; 4Z2V; X-ray; 1.39 A; A/B=21-154, C/P=153-164.
DR PDB; 4Z6J; X-ray; 2.40 A; A/B=21-164.
DR PDB; 6RTQ; X-ray; 2.00 A; A/B=20-164.
DR PDBsum; 4Z27; -.
DR PDBsum; 4Z28; -.
DR PDBsum; 4Z2O; -.
DR PDBsum; 4Z2P; -.
DR PDBsum; 4Z2V; -.
DR PDBsum; 4Z6J; -.
DR PDBsum; 6RTQ; -.
DR AlphaFoldDB; A9D857; -.
DR SMR; A9D857; -.
DR EnsemblBacteria; EDQ33228; EDQ33228; HPDFL43_17171.
DR eggNOG; ENOG502ZYDQ; Bacteria.
DR HOGENOM; CLU_1694061_0_0_5; -.
DR OrthoDB; 1588736at2; -.
DR Proteomes; UP000004291; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009374; F:biotin binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR Gene3D; 2.40.128.30; -; 1.
DR InterPro; IPR036896; Avidin-like_sf.
DR InterPro; IPR005468; Avidin/str.
DR Pfam; PF01382; Avidin; 1.
DR SUPFAM; SSF50876; SSF50876; 1.
DR PROSITE; PS51326; AVIDIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biotin; Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..164
FT /note="Hoefavidin"
FT /id="PRO_0000434588"
FT DOMAIN 32..155
FT /note="Avidin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00656"
FT BINDING 42
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000269|PubMed:26126731"
FT BINDING 46
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000269|PubMed:26126731"
FT BINDING 68..70
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000269|PubMed:26126731"
FT BINDING 76
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000269|PubMed:26126731"
FT BINDING 110..112
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000269|PubMed:26126731"
FT BINDING 148
FT /ligand="biotin"
FT /ligand_id="ChEBI:CHEBI:57586"
FT /evidence="ECO:0000269|PubMed:26126731"
FT DISULFID 77..108
FT /evidence="ECO:0000269|PubMed:26126731"
FT TURN 29..34
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 61..69
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:4Z2O"
FT TURN 90..93
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 104..119
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 121..124
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 126..137
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 140..153
FT /evidence="ECO:0007829|PDB:4Z2O"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:4Z2V"
SQ SEQUENCE 164 AA; 17412 MW; 66250B7CFF54B294 CRC64;
MNKVLAIVLT ITVAGFAQTA FADDHAMSPD MKLLAGASNW VNQSGSVAQF VFTPSPTQPQ
TYEVSGNYIN NAQGTGCKGT PYPLSGAYYS GNQIISFSVV WSNASANCQS ATGWTGYFDF
SGSQAVLKTD WNLAFYSGST PAIQQGQDDF MQSVATVSES LLTE
