IBP_FLAFP
ID IBP_FLAFP Reviewed; 276 AA.
AC H7FWB6; I3QNZ8;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2012, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=Ice-binding protein {ECO:0000303|PubMed:22750870, ECO:0000312|EMBL:AFK13196.1};
DE AltName: Full=Antifreeze protein {ECO:0000312|EMBL:EIA07191.1};
DE Short=AFP {ECO:0000305};
DE AltName: Full=FfIBP {ECO:0000303|PubMed:22750870};
DE Flags: Precursor;
GN ORFNames=HJ01_03463 {ECO:0000312|EMBL:EIA07191.1};
OS Flavobacterium frigoris (strain PS1).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1086011;
RN [1] {ECO:0000312|EMBL:AFK13196.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PS1 {ECO:0000312|EMBL:AFK13196.1};
RA Raymond J., Kim H.J.;
RT "An Antarctic sea ice bacterium that secretes ice-binding proteins.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:EIA07191.1, ECO:0000312|Proteomes:UP000005566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PS1 {ECO:0000312|EMBL:EIA07191.1,
RC ECO:0000312|Proteomes:UP000005566};
RA Raymond J., Kim H.J.;
RT "Flavobacterium frigoris PS1, a freeze-tolerant bacterium from Antarctic
RT sea ice.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP CRYSTALLIZATION OF 29-276, FUNCTION, AND SUBUNIT.
RC STRAIN=PS1 {ECO:0000303|PubMed:22750870};
RX PubMed=22750870; DOI=10.1107/s1744309112020465;
RA Do H., Lee J.H., Lee S.G., Kim H.J.;
RT "Crystallization and preliminary X-ray crystallographic analysis of an ice-
RT binding protein (FfIBP) from Flavobacterium frigoris PS1.";
RL Acta Crystallogr. F 68:806-809(2012).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASN-203.
RC STRAIN=PS1 {ECO:0000303|PubMed:27737617};
RX PubMed=27737617; DOI=10.1080/10826068.2016.1244682;
RA Kim E.J., Lee J.H., Lee S.G., Han S.J.;
RT "Improving thermal hysteresis activity of antifreeze protein from
RT recombinant Pichia pastoris by removal of N-glycosylation.";
RL Prep. Biochem. Biotechnol. 47:299-304(2017).
RN [5] {ECO:0007744|PDB:4NU2, ECO:0007744|PDB:4NU3, ECO:0007744|PDB:4NUH}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 61-276, X-RAY CRYSTALLOGRAPHY
RP (1.34 ANGSTROMS) OF 58-92; 91-132 AND 130-276 OF CHIMERA WITH FUNGAL
RP ANTIFREEZE PROTEIN, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP DOMAIN, MOTIF, DISULFIDE BOND, MUTAGENESIS OF THR-211; THR-234; ASN-248;
RP THR-251 AND THR-266, AND CIRCULAR DICHROISM ANALYSIS.
RC STRAIN=PS1 {ECO:0000312|EMBL:EIA07191.1};
RX PubMed=24699650; DOI=10.1107/s1399004714000996;
RA Do H., Kim S.J., Kim H.J., Lee J.H.;
RT "Structure-based characterization and antifreeze properties of a
RT hyperactive ice-binding protein from the Antarctic bacterium Flavobacterium
RT frigoris PS1.";
RL Acta Crystallogr. D 70:1061-1073(2014).
CC -!- FUNCTION: Has antifreeze activity for survival in a subzero
CC environment. Binds to the surface of ice crystals and inhibits their
CC growth. Has high thermal hysteresis (TH) activity, which is the ability
CC to lower the freezing point of an aqueous solution below its melting
CC point, and thus the freezing of the cell fluid can be prevented
CC protecting the organism from ice damage (PubMed:22750870,
CC PubMed:24699650, PubMed:27737617). The TH activity of this protein is
CC 2.2 degrees Celsius at 5 uM and 2.5 degrees Celsius at 50 uM
CC (PubMed:24699650). {ECO:0000269|PubMed:22750870,
CC ECO:0000269|PubMed:24699650, ECO:0000269|PubMed:27737617}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Active at low temperatures, even below 0 degree Celsius. Thermal
CC denaturation midpoint (Tm) is 56.4 degrees Celsius.
CC {ECO:0000269|PubMed:24699650};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22750870,
CC ECO:0000269|PubMed:24699650}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:27737617}.
CC -!- DOMAIN: The ice-binding site is formed by three T-A/G-X-T/N motifs.
CC {ECO:0000305|PubMed:24699650}.
CC -!- SIMILARITY: Belongs to the ice-binding protein family. {ECO:0000305}.
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DR EMBL; JQ712369; AFK13196.1; -; Genomic_DNA.
DR EMBL; AHKF01000032; EIA07191.1; -; Genomic_DNA.
DR RefSeq; WP_007139641.1; NZ_AHKF01000032.1.
DR PDB; 4NU2; X-ray; 2.10 A; A=29-276.
DR PDB; 4NU3; X-ray; 1.40 A; A/B=58-92, A/B=130-276.
DR PDB; 4NUH; X-ray; 1.34 A; A=91-132.
DR PDB; 7EHK; X-ray; 2.00 A; A=29-276.
DR PDBsum; 4NU2; -.
DR PDBsum; 4NU3; -.
DR PDBsum; 4NUH; -.
DR PDBsum; 7EHK; -.
DR AlphaFoldDB; H7FWB6; -.
DR SMR; H7FWB6; -.
DR STRING; 1086011.HJ01_03463; -.
DR EnsemblBacteria; EIA07191; EIA07191; HJ01_03463.
DR PATRIC; fig|1086011.3.peg.3394; -.
DR eggNOG; COG3420; Bacteria.
DR OMA; IFWQTAG; -.
DR OrthoDB; 1513508at2; -.
DR Proteomes; UP000005566; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR021884; Ice-bd_prot.
DR Pfam; PF11999; Ice_binding; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antifreeze protein; Disulfide bond; Secreted; Signal;
KW Stress response.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..276
FT /note="Ice-binding protein"
FT /evidence="ECO:0000255"
FT /id="PRO_5003610596"
FT MOTIF 79..82
FT /note="Ice-binding site motif (T-A/G-X-T/N) 1"
FT /evidence="ECO:0000305|PubMed:24699650"
FT MOTIF 245..248
FT /note="Ice-binding site motif (T-A/G-X-T/N) 2"
FT /evidence="ECO:0000305|PubMed:24699650"
FT MOTIF 263..266
FT /note="Ice-binding site motif (T-A/G-X-T/N) 3"
FT /evidence="ECO:0000305|PubMed:24699650"
FT SITE 251
FT /note="Ice-binding"
FT /evidence="ECO:0000269|PubMed:24699650"
FT DISULFID 107..124
FT /evidence="ECO:0000269|PubMed:24699650,
FT ECO:0007744|PDB:4NU2, ECO:0007744|PDB:4NUH"
FT MUTAGEN 203
FT /note="N->A,Q: Increased thermal hysteresis (TH) activity
FT compared to wild-type."
FT /evidence="ECO:0000269|PubMed:27737617"
FT MUTAGEN 211
FT /note="T->Y: No effect on thermal hysteresis (TH)
FT activity."
FT /evidence="ECO:0000269|PubMed:24699650"
FT MUTAGEN 234
FT /note="T->Y: No effect on thermal hysteresis (TH)
FT activity."
FT /evidence="ECO:0000269|PubMed:24699650"
FT MUTAGEN 248
FT /note="N->Y: Has 43% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:24699650"
FT MUTAGEN 251
FT /note="T->Y: Has 11% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:24699650"
FT MUTAGEN 266
FT /note="T->Y: Has 33% thermal hysteresis (TH) activity of
FT that of the wild-type."
FT /evidence="ECO:0000269|PubMed:24699650"
FT HELIX 68..72
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:4NUH"
FT HELIX 100..102
FT /evidence="ECO:0007829|PDB:4NUH"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:4NUH"
FT HELIX 129..148
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:4NUH"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 169..176
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:4NUH"
FT HELIX 218..220
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 254..263
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 265..269
FT /evidence="ECO:0007829|PDB:4NUH"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:4NUH"
SQ SEQUENCE 276 AA; 28447 MW; 24D0215A9C0D04D5 CRC64;
MKILKRIPVL AVLLVGLMTN CSNDSDSSSL SVANSTYETT ALNSQKSSTD QPNSGSKSGQ
TLDLVNLGVA ANFAILSKTG ITDVYKSAIT GDVGASPITG AAILLKCDEV TGTIFSVDAA
GPACKITDAS RLTTAVGDMQ IAYDNAAGRL NPDFLNLGAG TIGGKTLTPG LYKWTSTLNI
PTDITISGSS TDVWIFQVAG NLNMSSAVRI TLAGGAQAKN IFWQTAGAVT LGSTSHFEGN
ILSQTGINMK TAASINGRMM AQTAVTLQMN TVTIPQ
