HPE_HAEIN
ID HPE_HAEIN Reviewed; 160 AA.
AC P43961;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Surface-adhesin protein E;
DE Flags: Precursor;
GN Name=pe; OrderedLocusNames=HI_0178;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Acts as a multifunctional adhesin involved in direct
CC interactions with host epithelial cells and host proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}. Cell surface {ECO:0000250}.
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DR EMBL; L42023; AAC21855.1; -; Genomic_DNA.
DR PIR; F64003; F64003.
DR RefSeq; NP_438346.1; NC_000907.1.
DR RefSeq; WP_005694109.1; NC_000907.1.
DR PDB; 3ZH7; X-ray; 2.10 A; A=28-153.
DR PDBsum; 3ZH7; -.
DR AlphaFoldDB; P43961; -.
DR SMR; P43961; -.
DR STRING; 71421.HI_0178; -.
DR EnsemblBacteria; AAC21855; AAC21855; HI_0178.
DR KEGG; hin:HI_0178; -.
DR PATRIC; fig|71421.8.peg.182; -.
DR eggNOG; ENOG5031K7A; Bacteria.
DR HOGENOM; CLU_144598_0_0_6; -.
DR OMA; DSIWVDN; -.
DR BioCyc; HINF71421:G1GJ1-188-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR Gene3D; 2.40.128.710; -; 1.
DR InterPro; IPR043088; Adhesin_E.
DR InterPro; IPR031939; Adhesin_E-like.
DR InterPro; IPR016595; Adhesin_E_Pasteurellaceae.
DR Pfam; PF16747; Adhesin_E; 1.
DR PIRSF; PIRSF012320; Prplsmic_HI0178_prd; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal; Virulence.
FT SIGNAL 1..15
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 16..160
FT /note="Surface-adhesin protein E"
FT /id="PRO_0000013953"
FT LIPID 16
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 16
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3ZH7"
FT STRAND 46..58
FT /evidence="ECO:0007829|PDB:3ZH7"
FT STRAND 65..78
FT /evidence="ECO:0007829|PDB:3ZH7"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:3ZH7"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:3ZH7"
FT TURN 99..102
FT /evidence="ECO:0007829|PDB:3ZH7"
FT STRAND 103..115
FT /evidence="ECO:0007829|PDB:3ZH7"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3ZH7"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:3ZH7"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3ZH7"
FT HELIX 139..151
FT /evidence="ECO:0007829|PDB:3ZH7"
SQ SEQUENCE 160 AA; 18360 MW; D0F685EBCC9085DF CRC64;
MKKIILTLSL GLLTACSAQI QKAEQNDVKL APPTDVRSGY IRLVKNVNYY IDSESIWVDN
QEPQIVHFDA VVNLDRGLYV YPEPKRYARS VRQYKILNCA NYHLTQIRTD FYDEFWGQGL
RAAPKKQKKH TLSLTPDTTL YNAAQIICAN YGKAFSVDKK