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).
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| Accession Number: | Q8GM76 |
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| Protein Name: | Adhesin |
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| Length: | 1204 |
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| Molecular Weight: | 124783.00 |
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| Species: | Haemophilus influenzae [727] |
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| Substrate |
protein polypeptide chain |
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| Pfam: |
PF13018
PF05662
PF03895
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[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
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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