ID   HPI_DEIRA               Reviewed;         948 AA.
AC   P56867;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Hexagonally packed intermediate-layer surface protein;
DE   Flags: Precursor;
GN   Name=hpi; OrderedLocusNames=DR_2508;
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
CC   -!- FUNCTION: Shape maintenance, possible protection from noxious enzymes
CC       or exogenous and unsettling DNA, and may mediate homotypic cell-cell
CC       contacts. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer {ECO:0000250}.
CC       Note=This bacterium is covered by a S-layer with hexagonal symmetry.
CC       {ECO:0000250}.
CC   -!- PTM: Glycosylated. Contains tightly bound reducing sugars (six per
CC       polypeptide chain) and fatty acids (covalently bound and located in the
CC       N-terminal region) (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The hydrophilic C-terminal region rich in aromatic AA
CC       could be engaged in interactions with nucleic acids, and the bound
CC       fatty acids and the N-terminal region could serve to anchor the layer
CC       to the outer membrane of D.radiodurans. HPI layer contain about 30%
CC       beta structure and virtually no alpha helix (By similarity).
CC       {ECO:0000250}.
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; AE000513; AAF12049.1; -; Genomic_DNA.
DR   PIR; C75265; C75265.
DR   RefSeq; NP_296228.1; NC_001263.1.
DR   RefSeq; WP_010889133.1; NZ_CP015081.1.
DR   AlphaFoldDB; P56867; -.
DR   STRING; 243230.DR_2508; -.
DR   EnsemblBacteria; AAF12049; AAF12049; DR_2508.
DR   KEGG; dra:DR_2508; -.
DR   PATRIC; fig|243230.17.peg.2748; -.
DR   HOGENOM; CLU_310310_0_0_0; -.
DR   OrthoDB; 285019at2; -.
DR   Proteomes; UP000002524; Chromosome I.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Cell wall; Cell wall biogenesis/degradation; Disulfide bond; Glycoprotein;
KW   Lipoprotein; Reference proteome; S-layer; Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           18..948
FT                   /note="Hexagonally packed intermediate-layer surface
FT                   protein"
FT                   /id="PRO_0000032623"
FT   DISULFID        168..187
FT                   /evidence="ECO:0000250"
FT   DISULFID        554..666
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   948 AA;  99356 MW;  5CF0619F7AC97919 CRC64;
     MKKNIALMAL TGILTLASCG QNGTGTTPTA DACATANTCS VTVNISGVSS ADFDVTMDGK
     TTSMTLSNGQ KLPVAKTGTV TLTPKAKDGY TTPAAQSTTI SSTNLTPSVN FAYTTVPSTG
     NGNGNGGTTP TQPFTLNITS PTNGAAATTG TPIRVVFTSS VALSSATCKI GNSAAVNAQV
     SSTGGYCDVT PTTAGGGLIT VTGTANGQTV SSTVTVDVKA PVVDNRYGTV TPAGDQELTL
     TNEGIVKDAD NGWRRLGQGV STPSDPNGNV DIYVKGTVNF SVNAAAGSKV EVFLARTTGS
     DVPTNDDVQA GDVLRSVAST SGTETFSLDS RRLAEFDGVR KWIVVRINGT QVTYQPVIAD
     NKGPQQPDPE LNGVQNAYSN ILNNYNNSGL TYVRGDVNVF TGNPSLQDRE FGQAPLGSSF
     VQRRPSGFES IRYYLVPETA FGNKALQESD EMLRAKAIKS VATVVSAPVL EPGTVKATSF
     SRVIGSGATS TVTPKAQDNV TYRVYAISRD QLGNETASAT YELVRFDNVG PTITGSVIRD
     TSDLPFASQE PERCLSDIAT ITLGGITDNA GGVGLNPGQG LTFTLGGRQI QAGQFDTNQL
     ADGEYTIGFN SLTDALGNPV VSAPTNAKVY IDNTDPTVNF NRAVMQGTFA SGERVSVESD
     ASDGGCGVYE TRLFWDTDNG VVDDATTTPA IGHPVQFARQ RVTDGAKADS LNAGWNALQL
     PNGAGAVYLR ALVVDRAGNA TISTTPIVVN AKITNQARPL LGGFDAFKRN ASAQFMSNSN
     AISGVNGTAV TPNTTANSAL DNILSLDSVG TLTTNAYLPR GATETAITEK IRNVGAYGRF
     DATQWNRIRD YQLNTDPTLR SAYVNAGNLA NQRGNNWRIR TPWVELGSSD TANTQQKFDF
     NSDLLNDFYF GRTFGNNDNV NLFSYDQFNG IVSGTAGAYS FYGETVQK