HPI_DEIRD
ID HPI_DEIRD Reviewed; 1036 AA.
AC P13126;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Hexagonally packed intermediate-layer surface protein;
DE Flags: Precursor;
GN Name=hpi;
OS Deinococcus radiodurans.
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1299;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sark;
RX PubMed=3667529; DOI=10.1128/jb.169.11.5216-5223.1987;
RA Peters J., Peters M., Lottspeich F., Schaefer W., Baumeister W.;
RT "Nucleotide sequence analysis of the gene encoding the Deinococcus
RT radiodurans surface protein, derived amino acid sequence, and complementary
RT protein chemical studies.";
RL J. Bacteriol. 169:5216-5223(1987).
CC -!- FUNCTION: Shape maintenance, possible protection from noxious enzymes
CC or exogenous and unsettling DNA, and may mediate homotypic cell-cell
CC contacts.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer. Note=This bacterium
CC is covered by a S-layer with hexagonal symmetry.
CC -!- PTM: Glycosylated; contains six glycans.
CC -!- PTM: Acylated in the N-terminal region.
CC -!- PTM: The N-terminus is blocked.
CC -!- MISCELLANEOUS: The hydrophilic C-terminal region rich in aromatic amino
CC acids could be engaged in interactions with nucleic acids, and the
CC bound fatty acids and the N-terminal region could serve to anchor the
CC layer to the outer membrane of D.radiodurans. The HPI layer contains
CC about 30% beta structure and virtually no alpha helix.
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DR EMBL; M17895; AAA23335.1; -; Genomic_DNA.
DR PIR; A29832; A29832.
DR AlphaFoldDB; P13126; -.
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 Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW Cell wall; Cell wall biogenesis/degradation; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Lipoprotein; S-layer; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 18..1036
FT /note="Hexagonally packed intermediate-layer surface
FT protein"
FT /id="PRO_0000032624"
FT DISULFID 74..86
FT /evidence="ECO:0000269|PubMed:3667529"
FT DISULFID 256..275
FT /evidence="ECO:0000305"
FT DISULFID 642..754
FT /evidence="ECO:0000269|PubMed:3667529"
SQ SEQUENCE 1036 AA; 108028 MW; AAFF98206A74AEEE CRC64;
MKKNIALMAL TGVLTLASCG QNGNTPTADT TAPTVSLSVN NANLPSGVGS VVLSGTVNEA
STVVVKNNAG TTVCTVEVAA SGTFTCPATT IAGNTSTTST STSYTATATD AAKNVGTSSV
VTVNVAGVSN PAPTTAVLTI DLAGVSSAPI TIKDANGNVV QGYDNVTVND NATITVARGV
YTVTAGNVSG FNGPTTNFRV DLSGGNQTVT LNYTQAGTTT PTPVGSINIL TPAVGTSVTG
GSTVRVTFDK ANEVQCMVGG AAAVTAQVDS TSGYCDVVVP NSTGNVVITV MGKGVNGQTV
TATRNISVTQ AAVSYGVVTP AGDQELTLTS EGIVRDADSG WRRLGQGVST PSDPNLNLDI
YIKGTVNFSV NAPAGQKVEL FLARTTGSDV PTNDDIQAGD VLRSVASTSG TETFSLDSRR
LAEFDGVRKW IVVRINGTQV TYQPVIADNK GPQQPDPELN GVQNAYSNIL NNYNNSGLTY
VRGPVNVFTS NPSLQDREFG QAPVGSSFVQ RRPAGFESIR YYLVPESAFN NKALQESDEM
LRAKAVKSVA TVVSAPVLEP GTVKATSFSR VIGSGATSTV APKALDNVTY RVYAISRDQV
GNETASATYD LVRFDNVGPT ITGSVIRDTS DLPFPSQEPE RCLSDIATIS LGGIADNVGG
VGLNPGQGLT FTLGGRQIQA GQFDTNQLAD PEYTIGFNSL TDALGNPVVT APTNAKVYID
NTDPTVNFNR AVMQGTYASG GRVSVESDAS DGGCGVYETR LFWDTANGVV DDATTTPAIG
HPVQFARQRV TDGAKADSLN AGWNALQLPN GAGAVYLRSL VVDRAGNATI STTSIVVNAK
ITNQARPLLG GFDAFKRNAS AQFVGDDNVI AGVNGTAATP NVTGNSALDN ILSLDSVGTL
TTNAYLPRGA TETAITEKIR NVGAYGRFDA TQWNLIRDYQ LNTDPTLRSA YVNAGNLANQ
RGNNWRIRTP WVELGSSDTA NTQQKFDFNS DLLNDFYYGR TFGNNHSVNL FSYDQFNGVV
SDTAGAYSFY GETVRK