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ProGlyProt ID
BC147
Organism Information
Organism Name
Haemophilus influenzae 12
Domain
Bacteria
Classification
Family: Pasteurellaceae
Order: Pasteurellales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)
 
 
Genome Sequence(s)
EMBL
Organism Additional Information
Nonencapsulated (nontypeable) strains are human pathogens that colonize the upper respiratory tract to initiate infection. This results in localized respiratory and invasive disease.
 
 
Gene Information
Gene Name
hmw1
 
 
Protein Information
Protein Name
HMW1 (Adhesin)
UniProtKB/SwissProt ID
EMBL-CDS
UniProtKB Sequence
>tr|Q48031|Q48031_HAEIN Adhesin OS=Haemophilus influenzae GN=hmw1A PE=1 SV=1 MNK
IYRLKFSKRLNALVAVSELARGCDHSTEKGSEKPARMKVRHLALKPLSAMLLSLGVT SIPQSVLASGLQGMDVVH
GTATMQVDGNKTIIRNSVDAIINWKQFNIDQNEMVQFLQENN NSAVFNRVTSNQISQLKGILDSNGQVFLINPNG
ITIGKDAIINTNGFTASTLDISNENIK ARNFTFEQTKDKALAEIVNHGLITVGKDGSVNLIGGKVKNEGVISVNG
GSISLLAGQKIT ISDIINPTITYSIAAPENEAVNLGDIFAKGGNINVRAATIRNQGKLSADSVSKDKSGNIV LS
AKEGEAEIGGVISAQNQQAKGGKLMITGDKVTLKTGAVIDLSGKEGGETYLGGDERGE GKNGIQLAKKTSLEKGS
TINVSGKEKGGRAIVWGDIALIDGNINAQGSGDIAKTGGFVET SGHDLFIKDNAIVDAKEWLLDPDNVSINAETA
GRSNTSEDDEYTGSGNSASTPKRNKEKT TLTNTTLESILKKGTFVNITANQRIYVNSSINLSNGSLTLWSEGRSG
GGVEINNDITTGD DTRGANLTIYSGGWVDVHKNISLGAQGNINITAKQDIAFEKGSNQVITGQGTITSGNQKG F
RFNNVSLNGTGSGLQFTTKRTNKYAITNKFEGTLNISGKVNISMVLPKNESGYDKFKGR TYWNLTSLNVSESGEF
NLTIDSRGSDSAGTLTQPYNLNGISFNKDTTFNVERNARVNFDI KAPIGINKYSSLNYASFNGNISVSGGGSVDF
TLLASSSNVQTPGVVINSKYFNVSTGSSL RFKTSGSTKTGFSIEKDLTLNATGGNITLLQVEGTDGMIGKGIVAK
KNITFEGGNITFGS RKAVTEIEGNVTINNNANVTLIGSDFDNHQKPLTIKKDVIINSGNLTAGGNIVNIAGNLT
VESNANFKAITNFTFNVGGLFDNKGNSNISIAKGGARFKDIDNSKNLSITTNSSSTYRTI ISGNITNKNGDLNIT
NEGSDTEMQIGGDVSQKEGNLTISSDKINITKQITIKAGVDGENS DSDATNNANLTIKTKELKLTQDLNISGFNK
AEITAKDGSDLTIGNTNSADGTNAKKVTFN QVKDSKISADGHKVTLHSKVETSGSNNNTEDSSDNNAGLTIDAKN
VTVNNNITSHKAVSI SATSGEITTKTGTTINATTGNVEITAQTGSILGGIESSSGSVTLTATEGALAVSNISGNT
VTVTANSGALTTLAGSTIKGTESVTTSSQSGDIGGTISGGTVEVKATESLTTQSNSKIKA TTGEANVTSATGTI
GGTISGNTVNVTANAGDLTVGNGAEINATEGAATLTTSSGKLTTEA SSHITSAKGQVNLSAQDGSVAGSINAANV
TLNTTGTLTTVKGSNINATSGTLVINAKDAE LNGAALGNHTVVNATNANGSGSVIATTSSRVNITGDLITINGLN
IISKNGINTVLLKGVK IDVKYIQPGIASVDEVIEAKRILEKVKDLSDEEREALAKLGVSAVRFIEPNNTITVDTQ
N EFATRPLSRIVISEGRACFSNSDGATVCVNIADNGR
Sequence length
1536 AA
Subcellular Location
Surface
Function
High-molecular weight protein (virulence exoprotein) that is secreted by the bacterial two-partner secretion pathway and mediates adherence to respiratory epithelium, an essential early step in the pathogenesis.
 
 
Protein Structure
PDB ID
 
 
Glycosylation Status
Glycosylation Type
N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length Protein
N444, N484, N498, N546, N560, N570, N605, N609, N636, N642, N709, N773, N801, N806, N828, N835, N912, N928, N946, N952, N964, N973, N995, N1004, N1029, N1044, N1131, N1156, N1348, N1352, N1366,
Experimentally Validated Glycosite(s ) in Mature Protein
N444, N484, N498, N546, N560, N570, N605, N609, N636, N642, N709, N773, N801, N806, N828, N835, N912, N928, N946, N952, N964, N973, N995, N1004, N1029, N1044, N1131, N1156, N1348, N1352, N1366,
Glycosite(s) Annotated Protein Sequence
>tr|Q48031|Q48031_HAEIN Adhesin OS=Haemophilus influenzae GN=hmw1A PE=1 SV=1 MN
KIYRLKFSKRLNALVAVSELARGCDHSTEKGSEKPARMKVRHLALKPLSAMLLSLGVT SIPQSVLASGLQGMDV
VHGTATMQVDGNKTIIRNSVDAIINWKQFNIDQNEMVQFLQENN NSAVFNRVTSNQISQLKGILDSNGQVFLIN
PNGITIGKDAIINTNGFTASTLDISNENIK ARNFTFEQTKDKALAEIVNHGLITVGKDGSVNLIGGKVKNEGVI
SVNGGSISLLAGQKIT ISDIINPTITYSIAAPENEAVNLGDIFAKGGNINVRAATIRNQGKLSADSVSKDKSGN
IV LSAKEGEAEIGGVISAQNQQAKGGKLMITGDKVTLKTGAVIDLSGKEGGETYLGGDERGE GKNGIQLAKK
TSLEKGSTINVSGKEKGGRAIVWGDIALIDGNINAQGSGDIAKTGGFVET SGHDLFIKDNAIVDAKEWLLDPD
N*(444)
VSINAETAGRSNTSEDDEYTGSGNSASTPKRNKEKT TLTN*(484)TTLESILKKGTFVN*(4
98)
ITANQRIYVNSSINLSNGSLTLWSEGRSGGGVEINNDITTGD DTRGAN*(546)LTIYSGGWVDVHK
N*(560)
ISLGAQGNIN*(570)ITAKQDIAFEKGSNQVITGQGTITSGNQKG FRFNN*(605)VSLN
*(609)
GTGSGLQFTTKRTNKYAITNKFEGTLN*(636) ISGKVN*(642)ISMVLPKNESGYDKFKGR
TYWNLTSLNVSESGEFNLTIDSRGSDSAGTLTQPYNLNGISFNKDTTFN*(709)VERNARVNFDI KAPIG
INKYSSLNYASFNGNISVSGGGSVDFTLLASSSNVQTPGVVINSKYFN*(773)VSTGSSL RFKTSGSTKTG
FSIEKDLTLN*(801)ATGGN*(806)ITLLQVEGTDGMIGKGIVAKKN*(828)ITFEGGN*(835)
ITFGS RKAVTEIEGNVTINNNANVTLIGSDFDNHQKPLTIKKDVIINSGNLTAGGNIVNIAGNLT VESNANF
KAITN*(912)FTFNVGGLFDNKGNSN*(928)ISIAKGGARFKDIDNSKN*(946)LSITTN*(952)
SSSTYRTI ISGN*(964)ITNKNGDLN*(973)ITNEGSDTEMQIGGDVSQKEGN*(995)LTISSD
KIN*(1004)ITKQITIKAGVDGENS DSDATNNAN*(1029)LTIKTKELKLTQDLN*(1044)ISGF
NKAEITAKDGSDLTIGNTNSADGTNAKKVTFN QVKDSKISADGHKVTLHSKVETSGSNNNTEDSSDNNAGLTID
AKNVTVNNN*(1131)ITSHKAVSI SATSGEITTKTGTTIN*(1156)ATTGNVEITAQTGSILGGIESS
SGSVTLTATEGALAVSNISGNT VTVTANSGALTTLAGSTIKGTESVTTSSQSGDIGGTISGGTVEVKATESLTT
QSNSKIKA TTGEANVTSATGTIGGTISGNTVNVTANAGDLTVGNGAEINATEGAATLTTSSGKLTTEA SSHI
TSAKGQVNLSAQDGSVAGSINAAN*(1348)VTLN*(1352)TTGTLTTVKGSNIN*(1366)ATSGTLV
INAKDAE LNGAALGNHTVVNATNANGSGSVIATTSSRVNITGDLITINGLNIISKNGINTVLLKGVK IDVKY
IQPGIASVDEVIEAKRILEKVKDLSDEEREALAKLGVSAVRFIEPNNTITVDTQN EFATRPLSRIVISEGRACF
SNSDGATVCVNIADNGR
Sequence Around Glycosites (21 AA)
DAKEWLLDPDNVSINAETAGR
KRNKEKTTLTNTTLESILKKG
ESILKKGTFVNITANQRIYVN
ITTGDDTRGANLTIYSGGWVD
YSGGWVDVHKNISLGAQGNIN
NISLGAQGNINITAKQDIAFE
SGNQKGFRFNNVSLNGTGSGL
KGFRFNNVSLNGTGSGLQFTT
AITNKFEGTLNISGKVNISMV
EGTLNISGKVNISMVLPKNES
GISFNKDTTFNVERNARVNFD
PGVVINSKYFNVSTGSSLRFK
GFSIEKDLTLNATGGNITLLQ
KDLTLNATGGNITLLQVEGTD
MIGKGIVAKKNITFEGGNITF
AKKNITFEGGNITFGSRKAVT
ESNANFKAITNFTFNVGGLFD
GGLFDNKGNSNISIAKGGARF
ARFKDIDNSKNLSITTNSSST
DNSKNLSITTNSSSTYRTIIS
SSTYRTIISGNITNKNGDLNI
GNITNKNGDLNITNEGSDTEM
IGGDVSQKEGNLTISSDKINI
GNLTISSDKINITKQITIKAG
NSDSDATNNANLTIKTKELKL
TKELKLTQDLNISGFNKAEIT
IDAKNVTVNNNITSHKAVSIS
EITTKTGTTINATTGNVEITA
GSVAGSINAANVTLNTTGTLT
GSINAANVTLNTTGTLTTVKG
TLTTVKGSNINATSGTLVINA
Glycosite Sequence Logo
Glycosite Sequence Logo
Technique(s) used for Glycosylation Detection
Digoxygenin (DIG)-glycan detection
Technique(s) used for Glycosylated Residue(s) Detection
MS-MS (tandem mass spectrometry)
Protein Glycosylation- Implication
Glycosylation protects HMW1 against premature degradation during the process of secretion and facilitates HMW1 tethering to the bacterial surface, a prerequisite for HMW1-mediated adherence.
 
 
Glycan Information
Glycan Annotation
Unusual carbohydrate modification includes glucose, galactose, and possibly mannose and corresponds to 7–8 kDa of the molecular mass. 31 modification sites carry 47 hexose units indicating the presence of hexose and dihexose (162-Da) sugars. HMW1C is capable of transferring glucose and galactose to HMW1 and is also able to generate hexose-hexose bonds.
 
 
Protein Glycosylation linked (PGL) gene(s)
OST Gene Name
hmw1C (R2846_0712)
OST Protein Name
HMW1C (ApHMW1C Actinobacillus pleuropneumoniae)
OST UniProtKB/ SwissProt ID
OST EMBL-CDS
OST UniProtKB Sequence
Characterized Accessory Gene(s)
HMW1C is a novel glycosyltransferase that forms both hexose-hexose and hexose-Asn bonds.
 
 
Literature
Reference(s)
1) Choi, K.J., Grass, S., Paek, S., St Geme, J.W., 3rd and Yeo, H.J. (2010) The Actinobacillus pleuropneumoniae HMW1C-like glycosyltransferase mediates N-linked glycosylation of the Haemophilus influenzae HMW1 adhesin. PLoS One, 5, e15888. [PubMed: 21209858]
2) Grass, S., Lichti, C.F., Townsend, R.R., Gross, J. and St Geme, J.W., 3rd. (2010) The Haemophilus influenzae HMW1C protein is a glycosyltransferase that transfers hexose residues to asparagine sites in the HMW1 adhesin. PLoS Pathog, 6, e1000919. [PubMed: 20523900]
3) Gross, J., Grass, S., Davis, A.E., Gilmore-Erdmann, P., Townsend, R.R. and St Geme, J.W., 3rd. (2008) The Haemophilus influenzae HMW1 adhesin is a glycoprotein with an unusual N-linked carbohydrate modification. J Biol Chem, 283, 26010-26015. [PubMed: 18621734]
4) Yeo, H.J., Yokoyama, T., Walkiewicz, K., Kim, Y., Grass, S. and Geme, J.W., 3rd. (2007) The structure of the Haemophilus influenzae HMW1 pro-piece reveals a structural domain essential for bacterial two-partner secretion. J Biol Chem, 282, 31076-31084. [PubMed: 17699157]
5) Grass, S., Buscher, A.Z., Swords, W.E., Apicella, M.A., Barenkamp, S.J., Ozchlewski, N. and St Geme, J.W., 3rd. (2003) The Haemophilus influenzae HMW1 adhesin is glycosylated in a process that requires HMW1C and phosphoglucomutase, an enzyme involved in lipooligosaccharide biosynthesis. Mol Microbiol, 48, 737-751. [PubMed: 12694618]
Year of Identification
2003
Year of Validation
2008
 
 
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