ProGP228

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ProGP ID ProGP228
Validation Status Characterized
Organism Information
Organism NameHaemophilus influenzae 12
Domain Bacteria
Classification Family: Pasteurellaceae
Order: Pasteurellales
Class: Gammaproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI) 727
Genome Sequence(s)
EMBL U08876
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 Namehmw1
Protein Information
Protein NameHMW1 (Adhesin)
UniProtKB/SwissProt ID Q48031
EMBL-CDSAAA20527.1
UniProtKB Sequence >tr|Q48031|Q48031_HAEIN Adhesin OS=Haemophilus influenzae GN=hmw1A PE=1 SV=1 MNKIYRLKFSKRLNALVAVSELARGCDHSTEKGSEKPARMKVRHLALKPLSAMLLSLGVT SIPQSVLASGLQGMDVVHGTATMQVDGNKTIIRNSVDAIINWKQFNIDQNEMVQFLQENN NSAVFNRVTSNQISQLKGILDSNGQVFLINPNGITIGKDAIINTNGFTASTLDISNENIK ARNFTFEQTKDKALAEIVNHGLITVGKDGSVNLIGGKVKNEGVISVNGGSISLLAGQKIT ISDIINPTITYSIAAPENEAVNLGDIFAKGGNINVRAATIRNQGKLSADSVSKDKSGNIV LSAKEGEAEIGGVISAQNQQAKGGKLMITGDKVTLKTGAVIDLSGKEGGETYLGGDERGE GKNGIQLAKKTSLEKGSTINVSGKEKGGRAIVWGDIALIDGNINAQGSGDIAKTGGFVET SGHDLFIKDNAIVDAKEWLLDPDNVSINAETAGRSNTSEDDEYTGSGNSASTPKRNKEKT TLTNTTLESILKKGTFVNITANQRIYVNSSINLSNGSLTLWSEGRSGGGVEINNDITTGD DTRGANLTIYSGGWVDVHKNISLGAQGNINITAKQDIAFEKGSNQVITGQGTITSGNQKG FRFNNVSLNGTGSGLQFTTKRTNKYAITNKFEGTLNISGKVNISMVLPKNESGYDKFKGR TYWNLTSLNVSESGEFNLTIDSRGSDSAGTLTQPYNLNGISFNKDTTFNVERNARVNFDI KAPIGINKYSSLNYASFNGNISVSGGGSVDFTLLASSSNVQTPGVVINSKYFNVSTGSSL RFKTSGSTKTGFSIEKDLTLNATGGNITLLQVEGTDGMIGKGIVAKKNITFEGGNITFGS RKAVTEIEGNVTINNNANVTLIGSDFDNHQKPLTIKKDVIINSGNLTAGGNIVNIAGNLT VESNANFKAITNFTFNVGGLFDNKGNSNISIAKGGARFKDIDNSKNLSITTNSSSTYRTI ISGNITNKNGDLNITNEGSDTEMQIGGDVSQKEGNLTISSDKINITKQITIKAGVDGENS DSDATNNANLTIKTKELKLTQDLNISGFNKAEITAKDGSDLTIGNTNSADGTNAKKVTFN QVKDSKISADGHKVTLHSKVETSGSNNNTEDSSDNNAGLTIDAKNVTVNNNITSHKAVSI SATSGEITTKTGTTINATTGNVEITAQTGSILGGIESSSGSVTLTATEGALAVSNISGNT VTVTANSGALTTLAGSTIKGTESVTTSSQSGDIGGTISGGTVEVKATESLTTQSNSKIKA TTGEANVTSATGTIGGTISGNTVNVTANAGDLTVGNGAEINATEGAATLTTSSGKLTTEA SSHITSAKGQVNLSAQDGSVAGSINAANVTLNTTGTLTTVKGSNINATSGTLVINAKDAE LNGAALGNHTVVNATNANGSGSVIATTSSRVNITGDLITINGLNIISKNGINTVLLKGVK IDVKYIQPGIASVDEVIEAKRILEKVKDLSDEEREALAKLGVSAVRFIEPNNTITVDTQN EFATRPLSRIVISEGRACFSNSDGATVCVNIADNGR
Sequence length 1536 AA
Subcellular LocationSurface
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 2ODL
Glycosylation Status
Glycosylation Type N (Asn) linked
Experimentally Validated Glycosite(s) in Full Length ProteinN444, 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 ProteinN444, 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 MNKIYRLKFSKRLNALVAVSELARGCDHSTEKGSEKPARMKVRHLALKPLSAMLLSLGVT SIPQSVLASGLQGMDVVHGTATMQVDGNKTIIRNSVDAIINWKQFNIDQNEMVQFLQENN NSAVFNRVTSNQISQLKGILDSNGQVFLINPNGITIGKDAIINTNGFTASTLDISNENIK ARNFTFEQTKDKALAEIVNHGLITVGKDGSVNLIGGKVKNEGVISVNGGSISLLAGQKIT ISDIINPTITYSIAAPENEAVNLGDIFAKGGNINVRAATIRNQGKLSADSVSKDKSGNIV LSAKEGEAEIGGVISAQNQQAKGGKLMITGDKVTLKTGAVIDLSGKEGGETYLGGDERGE GKNGIQLAKKTSLEKGSTINVSGKEKGGRAIVWGDIALIDGNINAQGSGDIAKTGGFVET SGHDLFIKDNAIVDAKEWLLDPDN*(444)VSINAETAGRSNTSEDDEYTGSGNSASTPKRNKEKT TLTN*(484)TTLESILKKGTFVN*(498)ITANQRIYVNSSINLSNGSLTLWSEGRSGGGVEINNDITTGD DTRGAN*(546)LTIYSGGWVDVHKN*(560)ISLGAQGNIN*(570)ITAKQDIAFEKGSNQVITGQGTITSGNQKG FRFNN*(605)VSLN*(609)GTGSGLQFTTKRTNKYAITNKFEGTLN*(636) ISGKVN*(642)ISMVLPKNESGYDKFKGR TYWNLTSLNVSESGEFNLTIDSRGSDSAGTLTQPYNLNGISFNKDTTFN*(709)VERNARVNFDI KAPIGINKYSSLNYASFNGNISVSGGGSVDFTLLASSSNVQTPGVVINSKYFN*(773)VSTGSSL RFKTSGSTKTGFSIEKDLTLN*(801)ATGGN*(806)ITLLQVEGTDGMIGKGIVAKKN*(828)ITFEGGN*(835)ITFGS RKAVTEIEGNVTINNNANVTLIGSDFDNHQKPLTIKKDVIINSGNLTAGGNIVNIAGNLT VESNANFKAITN*(912)FTFNVGGLFDNKGNSN*(928)ISIAKGGARFKDIDNSKN*(946)LSITTN*(952)SSSTYRTI ISGN*(964)ITNKNGDLN*(973)ITNEGSDTEMQIGGDVSQKEGN*(995)LTISSDKIN*(1004)ITKQITIKAGVDGENS DSDATNNAN*(1029)LTIKTKELKLTQDLN*(1044)ISGFNKAEITAKDGSDLTIGNTNSADGTNAKKVTFN QVKDSKISADGHKVTLHSKVETSGSNNNTEDSSDNNAGLTIDAKNVTVNNN*(1131)ITSHKAVSI SATSGEITTKTGTTIN*(1156)ATTGNVEITAQTGSILGGIESSSGSVTLTATEGALAVSNISGNT VTVTANSGALTTLAGSTIKGTESVTTSSQSGDIGGTISGGTVEVKATESLTTQSNSKIKA TTGEANVTSATGTIGGTISGNTVNVTANAGDLTVGNGAEINATEGAATLTTSSGKLTTEA SSHITSAKGQVNLSAQDGSVAGSINAAN*(1348)VTLN*(1352)TTGTLTTVKGSNIN*(1366)ATSGTLVINAKDAE LNGAALGNHTVVNATNANGSGSVIATTSSRVNITGDLITINGLNIISKNGINTVLLKGVK IDVKYIQPGIASVDEVIEAKRILEKVKDLSDEEREALAKLGVSAVRFIEPNNTITVDTQN EFATRPLSRIVISEGRACFSNSDGATVCVNIADNGR
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
Technique(s) used for Glycosylation DetectionDigoxygenin (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 NameHMW1C (ApHMW1C Actinobacillus pleuropneumoniae)
OST ProGT IDProGT43
Characterized Accessory Gene(s)HMW1C is a novel glycosyltransferase that forms both hexose-hexose and hexose-Asn bonds.
Literature
Year of Identification2003
Year of Identification Month Wise2003.5.1
Year of Validation 2008
Reference 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]
Author Grass, S., Buscher, A.Z., Swords, W.E., Apicella, M.A., Barenkamp, S.J., Ozchlewski, N. St Geme, J.W., 3rd.
Research GroupThe Edward Mallinckrodt Department of Pediatrics and Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Ave., Campus Box 8208, St Louis, MO 63110, USA.
Corresponding Author St Geme, J.W., 3rd.
ContactThe Edward Mallinckrodt Department of Pediatrics and Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Ave., Campus Box 8208, St Louis, MO 63110, USA.
Reference 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]
Author Grass, S., Lichti, C.F., Townsend, R.R., Gross, J. St Geme, J.W., 3rd.
Research GroupDepartment of Pediatrics, Duke University Medical Center, Durham, North Carolina, United States of America.
Corresponding Author St Geme, J.W., 3rd.
ContactDepartment of Pediatrics, Duke University Medical Center, Durham, North Carolina, United States of America.
Reference 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]
Author Grass, S., Lichti, C.F., Townsend, R.R., Gross, J. St Geme, J.W., 3rd.
Research GroupDepartment of Pediatrics, Duke University Medical Center, Durham, North Carolina, United States of America
Corresponding Author St Geme, J.W., 3rd.
ContactDepartment of Pediatrics, Duke University Medical Center, Durham, North Carolina, United States of America
Reference 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]
Author Gross, J., Grass, S., Davis, A.E., Gilmore-Erdmann, P., Townsend, R.R. and St Geme, J.W., 3rd.
Research GroupDepartment of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Corresponding Author St Geme, J.W., 3rd.
ContactDepartment of Medicine, Washington University School of Medicine, St. Louis, Missouri 63110, USA.
Reference 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]
Author Yeo, H.J., Yokoyama, T., Walkiewicz, K., Kim, Y., Grass, S. and Geme, J.W.,
Research GroupDepartment of Biology and Biochemistry, University of Houston, Houston, Texas 77204, USA. hyeo@uh.edu
Corresponding Author Geme, J.W., 3rd.
ContactDepartment of Biology and Biochemistry, University of Houston, Houston, Texas 77204, USA. hyeo@uh.edu
Reference1) 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]
AuthorChoi, K.J., Grass, S., Paek, S., St Geme, J.W., 3rd and Yeo, H.J.
Research GroupDepartment of Biology and Biochemistry, University of Houston, Houston, Texas, United States of America.
Corresponding Author Yeo, H.J.
ContactDepartment of Biology and Biochemistry, University of Houston, Houston, Texas, United States of America.