ID   ICEN_XANCT              Reviewed;        1567 AA.
AC   P18127;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Ice nucleation protein;
GN   Name=inaX;
OS   Xanthomonas campestris pv. translucens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=343;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=X56S;
RX   PubMed=2259339; DOI=10.1007/bf00315811;
RA   Zhao J., Orser C.S.;
RT   "Conserved repetition in the ice nucleation gene inaX from Xanthomonas
RT   campestris pv. translucens.";
RL   Mol. Gen. Genet. 223:163-166(1990).
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 153 imperfect repeats of a consensus octapeptide A-G-
CC       Y-G-S-T-L-T; further on a 16-residue and a regional 48-residue
CC       periodicity is superimposed.
CC   -!- MISCELLANEOUS: A structural model is suggested in which the ice
CC       nucleation protein displays a symmetry related to that of ice.
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; X52970; CAA37140.1; -; Genomic_DNA.
DR   RefSeq; WP_058197395.1; NZ_LNVU01000049.1.
DR   AlphaFoldDB; P18127; -.
DR   BMRB; P18127; -.
DR   STRING; 1205753.A989_14712; -.
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; 26.
DR   PRINTS; PR00327; ICENUCLEATN.
DR   PROSITE; PS00314; ICE_NUCLEATION; 57.
PE   3: Inferred from homology;
KW   Cell outer membrane; Ice nucleation; Membrane; Repeat.
FT   CHAIN           1..1567
FT                   /note="Ice nucleation protein"
FT                   /id="PRO_0000204027"
FT   REGION          130..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          356..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          449..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          502..529
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          594..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..668
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          689..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          738..764
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          785..810
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..860
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          929..959
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          977..1004
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        136..180
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1567 AA;  152549 MW;  C8B451D959ECAD63 CRC64;
     MIVEKILALR TCANNMADHC GLIWPMAGPV ECKFWKPSGL HENGLTGLLW GKGVGAHLSA
     HADARWVVCE VAVDEMLQLA EEGMIKFPRA TVLFVGNRSQ ALDYIAANMP LYGAALQLAA
     PAAPAHVHMP AAEPSAPATQ ATSATLPTPA TPSTQATPST QSTQSTQSTE ATQSTEATPV
     ATVAAAPPPP GQQHDVMAKK TETGVYGSTL TGADQSRLVA GYGSTETAGD HSDLIAGYGS
     TGTAGSDSSI LAGYGSTQTA AGRSTLTAGY GSTQTAQEGS RLTSGYGSTA TSGSDSAVIS
     GYGSTQTAGS ESSLTAGYGS TQTARKGSDI TAGYGSTGTA GSDSALIAGY GSTQTAGSES
     SLTAGYGSTQ TARKGSDVTA GYGSTGTAGA DSTLIAGYGS TQTAGGESSL TAGYGSTQTA
     RQGSDITAGY GSTGTAGADS TLIAGYGSTQ TSGSDSSLTA GYGSTQTARK GSDITAGYGS
     TGTAGSDSSL IAGYGSTQTA GSESSLTAGY GSTQTAQQDS SLTTGYGSTS TAGHDSSLIA
     GYGSTQTAGY DSTLTAGYGS TQTAQQDSSL TTGYGSTSTA GADSTLIAGY GSTQTAGSDS
     SLTAGYGSTQ TAREGSDVTA GYGSTGTAGA DSTLIAGYGS TQTSGSDSSL TAGYGSTQTA
     RKGSDVTAGY GSTGTAGADS TLIAGYGSTQ TSGSDSSLTA GYGSTQTARK GSDVTAGYGS
     TGTAGADSTL IAGYGSTQTS GSDSSLTAGY GSTQTARKGS DVTAGYGSTG TAGADSTLIA
     GYGSTQTSGS DSSLTAGYGS TQTARKGSDI TAGYGSTGTA GADSTLIAGY GSTQTSGSDS
     SLTAGYGSTQ TAREGSDVTA GYGSTGTAGA DSTLISGYGS TQTAGSDSSL TAGYGSTQTA
     RKGSDVTAGY GSTGTAGADS TLIAGYGSTQ TSGSDSSLTA GYGSTQTARK GSDMTAGYGS
     TGTAGADSTL IAGYGSTQTS GSDSSLTAGY GSTQTAREGS DVTAGYGSTG TAGADSTLIA
     GYGSTQTAGS DSSLTAGYGS TQTARQGSDV TAGYGSTGTA GADSTLIAGY GSTQTAGSDS
     SLTAGYGSTQ TARQGSDITA GYGSTGTAGA DSSLIAGYGS TQTAGYDSNL TAGYGSTQTA
     REDSSLTAGY GSTSTAGHDS SLIAGYGSTQ TAGYNSILTT GYGSTQTAQE SSSLTAGYGS
     TSTAGYDSTL TAGYGSTQTA GYKSTLTAGY GSNSTAGHES SLIAGYGSTQ IAGYESTLTA
     GYGSSLTTQQ NSSLTAGYGS TEIAGYASTL MAGYGSSQTA GYESTLTAGY GSTQMAEHSS
     SLTAGYGSTG IAGQDSSLIA GYGSSLTSGV RSFLTAGYGS NMIASYGSSL IAGHECTQIA
     GHKSMLIAGK GSFQTAGARS TLIGGAASVQ TAGDRSKLIA GADSTQTAGD RSKLLAGRNS
     YLTAGDRSKL TAGDDSTLMA GDRSKLTAGK NSVLTAGANS RLIGSLGSTL SGGENSTLIF
     RCWDGERYTN LVVRTGEQGV ESDIPYQVDD EGNLVGKADD DLVLDYDPGM ILDGQCSPGT
     GEELRDV