IBP1_SHEFN
ID IBP1_SHEFN Reviewed; 892 AA.
AC Q086E4;
DT 12-SEP-2018, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Ice-binding protein 1 {ECO:0000303|PubMed:29498209};
DE AltName: Full=Antifreeze protein 1 {ECO:0000305};
DE Short=AFP 1 {ECO:0000305};
DE AltName: Full=Ice adhesin 1 {ECO:0000303|PubMed:29498209};
DE Flags: Precursor;
GN OrderedLocusNames=Sfri_1018 {ECO:0000312|EMBL:ABI70871.1};
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167 {ECO:0000312|EMBL:ABI70871.1};
RN [1] {ECO:0000312|EMBL:ABI70871.1, ECO:0000312|Proteomes:UP000000684}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400 {ECO:0000312|EMBL:ABI70871.1,
RC ECO:0000312|Proteomes:UP000000684};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0007744|PDB:6BG8}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 656-892, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=NCIMB 400 {ECO:0000303|PubMed:29498209};
RX PubMed=29498209; DOI=10.1111/febs.14424;
RA Vance T.D.R., Graham L.A., Davies P.L.;
RT "An ice-binding and tandem beta-sandwich domain-containing protein in
RT Shewanella frigidimarina is a potential new type of ice adhesin.";
RL FEBS J. 285:1511-1527(2018).
CC -!- FUNCTION: Ice-binding adhesion protein that adsorbs this bacterium onto
CC ice to maintain a favorable position in its aquatic habitat. Inhibits
CC growth of the ice crystals. Has high thermal hysteresis (TH) activity,
CC which is the ability to lower the freezing point of an aqueous solution
CC below its melting point. The TH activity of this protein is
CC approximately 1.4 degrees Celsius at 25 uM and little below 2 degrees
CC Celsius at 80 uM. {ECO:0000269|PubMed:29498209}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000305|PubMed:29498209}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303}; Extracellular side {ECO:0000305|PubMed:29498209}.
CC -!- SIMILARITY: Belongs to the ice-binding protein family. {ECO:0000305}.
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DR EMBL; CP000447; ABI70871.1; -; Genomic_DNA.
DR RefSeq; WP_011636492.1; NC_008345.1.
DR PDB; 6BG8; X-ray; 1.60 A; A/B=656-892.
DR PDBsum; 6BG8; -.
DR AlphaFoldDB; Q086E4; -.
DR SMR; Q086E4; -.
DR STRING; 318167.Sfri_1018; -.
DR EnsemblBacteria; ABI70871; ABI70871; Sfri_1018.
DR KEGG; sfr:Sfri_1018; -.
DR eggNOG; COG4932; Bacteria.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_323877_0_0_6; -.
DR OMA; YGTMSAT; -.
DR OrthoDB; 11082at2; -.
DR Proteomes; UP000000684; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR003343; Big_2.
DR InterPro; IPR021884; Ice-bd_prot.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR Pfam; PF02368; Big_2; 6.
DR Pfam; PF11999; Ice_binding; 1.
DR SMART; SM00635; BID_2; 7.
DR SUPFAM; SSF49373; SSF49373; 5.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antifreeze protein; Cell outer membrane; Lipoprotein;
KW Membrane; Palmitate; Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..892
FT /note="Ice-binding protein 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT /id="PRO_5004166303"
FT DOMAIN 43..111
FT /note="BIG2 1"
FT /evidence="ECO:0000255"
FT DOMAIN 134..205
FT /note="BIG2 2"
FT /evidence="ECO:0000255"
FT DOMAIN 221..288
FT /note="BIG2 3"
FT /evidence="ECO:0000255"
FT DOMAIN 306..386
FT /note="BIG2 4"
FT /evidence="ECO:0000255"
FT DOMAIN 392..471
FT /note="BIG2 5"
FT /evidence="ECO:0000255"
FT DOMAIN 478..558
FT /note="BIG2 6"
FT /evidence="ECO:0000255"
FT DOMAIN 565..638
FT /note="BIG2 7"
FT /evidence="ECO:0000255"
FT MOTIF 866..869
FT /note="Ice-binding site motif (T-A/G-X-T/N)"
FT /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT SITE 866
FT /note="Ice-binding"
FT /evidence="ECO:0000250|UniProtKB:H7FWB6"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT HELIX 663..667
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 668..678
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 683..694
FT /evidence="ECO:0007829|PDB:6BG8"
FT HELIX 696..698
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 699..701
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 714..716
FT /evidence="ECO:0007829|PDB:6BG8"
FT TURN 726..728
FT /evidence="ECO:0007829|PDB:6BG8"
FT HELIX 738..757
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 758..760
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 766..768
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 777..787
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 789..791
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 796..799
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 808..814
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 816..818
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 825..828
FT /evidence="ECO:0007829|PDB:6BG8"
FT HELIX 833..835
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 836..842
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 844..846
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 851..860
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 862..864
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 869..885
FT /evidence="ECO:0007829|PDB:6BG8"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:6BG8"
SQ SEQUENCE 892 AA; 89965 MW; F00A53F67E882AFE CRC64;
MNHSIKKTYL VFTMLLGFIL LAGCNGDNNN DNSNNDNNGV LLTSIAVTPA TPSMPLGLKQ
QFTAMGTYSD GTSSDITNSA TWSSDDSTVA TINGSGLAMG VIPGSVAITA SLIDSSSNEQ
SATTTLTITD ATLTALAITP VNPSLAKGLT KQFMATGTYS DGTSPDVTTS VTWSSANTLV
ATVNASGLAS GVAIGSSIIT ASLGSDETTT ELNITDAILS SIALTPVEPS IAKGITQQFT
AIGTYSDGIS VDITASSNWS SADTLVATMN TSGAAKGVSI GSSIITADFQ AQSATSLLTV
TDASLTSIML TPANPHIPKG NTLQLTATGI YSDGISVDIT SSAIWSSADT LIATVNADGV
VSGITSGSAI ITATSAALSA TTTVTVTDTT LTSIAVTPGN QTIVKGSNKQ LTATGTYSDG
SLANITASVT WSSADTLVAT VNNSGLASGI ETGSSLISAS SGALSGSTNL TITGAALNSI
VVSPTNLSLV KGMNKQFAAT ATYSDGSVAD ISTSVTWSSA DTLVATIDVN GLANGKAAGS
SLITATSGAQ SNSTNLTVTD ATLNSIDVTP INPSIIKNSS QNFVATGHYS DGSTTNITST
VMWSSADTLV ATLNPNEQLN SGRATAIEVG SSVIQASLSG VFADTTLNVT AALPNNPLAP
ELGEVARFAM LASQAITTTS GSAIVDGDLG ILDQARSYYA GFTPGVNAGE FDELTNGLSY
AGDDSTPPYV VPVPYASMVA FINQSRTDLG IAYNFLAADP NPNAATQVCP IELGNLTLTR
GVYKTAADVT LQTGTLTLDG EGDPDSVFIF TIGGNLTSGA PGGDIVLING AQAKNIYWRT
AGKTVIGTNT NFSGNVFAWS EVNVRTGANV TGRLFAVTDQ VTLDANAVTK AN
