ICEA_PANAN
ID ICEA_PANAN Reviewed; 1322 AA.
AC P20469;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Ice nucleation protein InaA;
GN Name=inaA;
OS Pantoea ananas (Erwinia uredovora).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=553;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2599095; DOI=10.1016/0014-5793(89)81678-3;
RA Abe K., Watabe S., Emori Y., Watanabe M., Arai S.;
RT "An ice nucleation active gene of Erwinia ananas. Sequence similarity to
RT those of Pseudomonas species and regions required for ice nucleation
RT activity.";
RL FEBS Lett. 258:297-300(1989).
CC -!- FUNCTION: Ice nucleation proteins enable bacteria to nucleate
CC crystallization in supercooled water.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Peripheral
CC membrane protein {ECO:0000250}.
CC -!- DOMAIN: Contains many imperfect repeats of a consensus octapeptide A-G-
CC Y-G-S-T-X-T; further on a 16-residue and a regional 48-residue
CC periodicity is superimposed.
CC -!- SIMILARITY: Belongs to the bacterial ice nucleation protein family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X17316; CAA35194.1; -; Genomic_DNA.
DR PIR; S07053; S07053.
DR AlphaFoldDB; P20469; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050825; F:ice binding; IEA:UniProtKB-KW.
DR InterPro; IPR000258; Ice_nucleatn.
DR Pfam; PF00818; Ice_nucleation; 25.
DR PRINTS; PR00327; ICENUCLEATN.
DR PROSITE; PS00314; ICE_NUCLEATION; 49.
PE 3: Inferred from homology;
KW Cell outer membrane; Ice nucleation; Membrane; Repeat.
FT CHAIN 1..1322
FT /note="Ice nucleation protein InaA"
FT /id="PRO_0000204021"
FT REGION 162..1281
FT /note="Octapeptide periodicity"
FT REGION 271..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 327..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1322 AA; 131095 MW; 89B0EE24AA837039 CRC64;
MKEDKVLILR TCANNMADHG GIIWPLSGIV ECKYWKPVKG FENGLTGLIW GKGSDSPLSL
HADARRVVAE VAADECIAIE THGWIKFPRA EVLHVGTQNS AMQFILHHRA DYVACTEMQA
GPGGPDVTSE AKAGNRSLPV TDDIDATIES GSTQPTQTIE IATYGSTLSG THQSQLIAGY
GSTETAGDSS TLIAGYGSTG TAGSDSTLVA GYGSTQTAGE ESSQMAGYGS TQTGMKGSDL
TAGYGSTGTA GADSSLIAGY GSTQTAGEDN SLTAGYGSTQ TAGEDSSLTA GYGSTQTAQK
GSDLTAGYGS TGTAGADSSL IAGYGSTQTA GEESTQTAGY GSTQTAQKGS DLTAGYGSTG
TAGDDSSLIA GYGSTQTAGE DSSLTAGYGS TQTAQKGSDL TAGYGSTGTS GADSSLIAGY
GSTQTAGEES TQTAGYGSTQ TAQKGSDLTA GYGSTGTAGD DSSLIAGYGS TQTAQKGSDL
TAGYGSTSTA GYESSLIAGY GSTQTAGYGS TLTAGYGSTQ TAQNESDLIT GYGSTSTAGA
NSSLIAGYGS TQTASYNSVL TAGYGSTQTA REGSDLTAGY GSTGTAGSDS SIIAGYGSTS
TAGADSSLIA GYGSTQTAGY NSILTAGYGS TQTAEEGSDL TAGYGSTSTA GADSSLIAGY
GSTQTAGYNS ILTAGYGSTQ TAQEGSDLTA GYGSTSTAGA DSSLIAGYGS TQTASYHSSL
TAGYGSTQTA QEQSVLTTGY GSTSTAGADS SLIAGYGSTQ TAGYNSILTA GYGSTQTAQE
RSDLTTGYGS TSTAGADSSL IAGYGSTQTA GYHSILTAGY GSTQTAQERS DLTTGYGSTS
TAGADSSLIA GYGSTQTAGY NSILTAGYGS TQTAQENSDL TTGYGSTSTA GYDSSLIAGY
GSTQTAGYHS ILTAGYGSTQ TARTRSDLTT GYGSTSTAGP DSSLIAGYGS TQTAGYNSIL
TAGYGSTQTG QENSDLTTGY GSTSTAGYES SLIAGYGSTQ TASFKSTLMA GYGSSQTARE
QSSLTAGYGS TSMAGYDSSL IAGYGSTQTA GYQSTLTAGY GSTQTAEHSS TLTAGYGSTA
TAGADSSLIA GYGSSLTSGI RSFLTAGYGS TLISGLRSVL TAGYGSSLIS GRRSSLTAGY
GSNQIASHRS SLIAGPESTQ ITGNRSMLIA GKGSSQTAGY RSTLISGADS VQMAGERGKL
IAGADSTQTA GDRSKLLAGN NSYLTAGDRS KLTAGNDCIL MAGDRSKLTA GINSILTAGC
RSKLIGSNGS TLTAGENSVL IFRCWDGKRY TNVVAKTGKG GIEADMPYQM DEDNNIVNKP
EE