(data stored in ACNUC7421 zone)

SWISSPROT: 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   11-DEC-2019, entry version 61.
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:0000244|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}.
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   SMR; Q086E4; -.
DR   STRING; 318167.Sfri_1018; -.
DR   EnsemblBacteria; ABI70871; ABI70871; Sfri_1018.
DR   KEGG; sfr:Sfri_1018; -.
DR   eggNOG; ENOG4107VGF; Bacteria.
DR   eggNOG; ENOG410ZW5J; LUCA.
DR   OMA; YGTMSAT; -.
DR   OrthoDB; 11082at2; -.
DR   BioCyc; SFRI318167:G1G77-1051-MONOMER; -.
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-like.
DR   InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR   Pfam; PF02368; Big_2; 6.
DR   Pfam; PF11999; DUF3494; 1.
DR   SMART; SM00635; BID_2; 7.
DR   SUPFAM; SSF49373; SSF49373; 5.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q086E4.
DR   SWISS-2DPAGE; Q086E4.
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:0000244|PDB:6BG8"
FT   STRAND          668..678
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          683..694
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   HELIX           696..698
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          699..701
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          714..716
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   TURN            726..728
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   HELIX           738..757
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          758..760
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          766..768
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          777..787
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          789..791
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          796..799
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          808..814
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          816..818
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          825..828
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   HELIX           833..835
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          836..842
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          844..846
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          851..860
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          862..864
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          869..885
FT                   /evidence="ECO:0000244|PDB:6BG8"
FT   STRAND          887..890
FT                   /evidence="ECO:0000244|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
//

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