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1.B.40.2.4
Adhesin (Hia) The 3-d structure is available (PDB#2GR7). Mediates bacterial adhesion to the respiratory epithelium. The crystal structure of the C-terminal end of Hia, corresponding to the entire Hia translocator domain and part of the passenger domain (residues 992-1098) shows that this domain forms a beta-barrel with 12 transmembrane beta-strands, including four strands from each subunit. The beta-barrel has a central channel of 1.8 nm in diameter that is traversed by three N-terminal alpha-helices, one from each subunit. Mutagenesis studies demonstrated that the transmembrane portion of the three alpha-helices and the loop region between the alpha-helices and the neighboring beta-strands are essential for stability, and that trimerization of the translocator domain is a prerequisite for translocator activity (Meng et al. 2006).  Electrostatic repulsion between the positive charges of Arg1077 is important to prevent the formation of misassembled oligomers by the Hia transmembrane domain in vitro (Aoki et al. 2017).

Accession Number:Q8GM76
Protein Name:Adhesin
Length:1204
Molecular Weight:124783.00
Species:Haemophilus influenzae [727]
Substrate proteins

Cross database links:

Pfam: PF13018    PF05662    PF03895   

Gene Ontology

GO:0019867 C:outer membrane
GO:0009405 P:pathogenesis

References (1)

[1] “The Haemophilus influenzae Hia autotransporter harbours two adhesive pockets that reside in the passenger domain and recognize the same host cell receptor.”  Laarmann S.et.al.   12410830

External Searches:

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  • 2° Structure (Network Protein Sequence Analysis)

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Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MNKIFNVIWN IVTQTWVVVS ELTRTHTKCA SATVAVAVLA TLLSATVEAN NSTSVTSKLN 
61:	VYGDTNTNFD AANNSIADLN KQNDGVHNGL LNLNEKGSGK NLLVSDNTAA TVGDLRKLGW 
121:	VVSTKNGTEE KSSQVKQADE VLFTGSGAAT VSSSSKDGKH TITVSVTKGS FADVKTDATT 
181:	TGQVNADRGK VKAADENGAD ADKKVATVKD VAKAINGAAT FVKVESDNTE ISDTDKADDG 
241:	TNDALKAGDT LTLKAGKNLK VKRTNKEVTF ALTKDLDVKT ATVSDTLTIG GNKDAGGTAT 
301:	PKINITSTAQ GLNFAKDGKT GNDANIHLNG IASTLTDTLT GASTTKVEKD TDKITDEEKA 
361:	RAASIQDVFN AGWNIKGVKT GATTSDNVDF VRTYDTVEFL SGSEETTMVT VDSESNGKST 
421:	KVKIGAKTSV IKEKDGKLFT GKANKDTNQV ASNNAADDTD EGKGLVTAET VINAVNKAGW 
481:	RIKTTGANNQ AGQFETVTSG TNVTFADGNG TTAVVTGDAT NGITVKYEAK VGDGLKIGND 
541:	QKITADTTAL TVTGGKVTAP DATNGKKLVN ASGLADALNK LSWTAKAEAD TANGGELDGT 
601:	ADEKEVKAGE TVTFKAGKNL KVKQDGANFT YSLKDTLTGL TSITLNDATA NGGNGAKTEI 
661:	TKDGLTITPA NGAGTNNANI ISVTTSGISA GNKAITNVAS GLNAYGDTNT NFDATANSAT 
721:	DLTRQFDANG AYDGLLNLNE KGANKNLLVA DSTAATVGDL RGLGWVISAD KTTGELNKEY 
781:	NAQVRNANEV KFKSGNGINV SGKTVNGTHE ITFELAKGEV VKSNEFTVKE TNGKETSLVK 
841:	VGDKYYSKED IDPATGNPKV TNGNAVTAKY QTQGNKIVST DGNNTEVTLT NKGSGYVTGN 
901:	QVADAIAKSG FELGLANETE AKAAFGDKEK TLSDTKLETV NAHDKVRFAN GLNTKVSAAT 
961:	VESTDANGDK VTTTFVKTDV ELPLTQIYNT DANGKKIVKK ADGKWYEVNT DGTVSNTEVT 
1021:	LGNVDANGKK VVKEDNKWYH VKSDGSTDKT QVVEEAKVST DEKHVVSLDP NGQSKGKGVV 
1081:	IDNVANGDIS ATSTDAINGS QLYAVAKGVT NLAGQVNNLE GKVNKVGKRA DAGTASALAA 
1141:	SQLPQATMPG KSMVAIAGSS YQGQNGLAIG VSRISDNGKV IIRLSGTTNS QGKTGVAAGV 
1201:	GYQW