ID   HPF_HAEI3               Reviewed;         293 AA.
AC   A4N8V8;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 48.
DE   RecName: Full=Putative metal ABC transporter substrate-binding protein Hpf;
DE   AltName: Full=Surface-adhesin protein F;
DE   Flags: Precursor;
GN   Name=hpf; ORFNames=CGSHi3655_02309;
OS   Haemophilus influenzae (strain NTHi 3655).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=375177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTHi 3655;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
RN   [2]
RP   FUNCTION IN VIRULENCE, INTERACTION WITH LAMININ, SUBCELLULAR LOCATION, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=NTHi 3655;
RX   PubMed=23230060; DOI=10.1093/infdis/jis754;
RA   Jalalvand F., Su Y.C., Morgelin M., Brant M., Hallgren O.,
RA   Westergren-Thorsson G., Singh B., Riesbeck K.;
RT   "Haemophilus influenzae protein F mediates binding to laminin and human
RT   pulmonary epithelial cells.";
RL   J. Infect. Dis. 207:803-813(2013).
RN   [3]
RP   FUNCTION IN VIRULENCE, INTERACTION WITH VITRONECTIN, SUBCELLULAR LOCATION,
RP   AND DISRUPTION PHENOTYPE.
RC   STRAIN=NTHi 3655;
RX   PubMed=23387957; DOI=10.1111/mmi.12164;
RA   Su Y.C., Jalalvand F., Morgelin M., Blom A.M., Singh B., Riesbeck K.;
RT   "Haemophilus influenzae acquires vitronectin via the ubiquitous Protein F
RT   to subvert host innate immunity.";
RL   Mol. Microbiol. 87:1245-1266(2013).
CC   -!- FUNCTION: Part of an ATP-driven transport system for iron. Metal-
CC       binding component (Potential). Acts as an adhesin that promotes binding
CC       of H.influenzae to host laminin and vitronectin. In addition,
CC       interaction with serum vitronectin plays an important role in bacterial
CC       serum resistance. {ECO:0000269|PubMed:23230060,
CC       ECO:0000269|PubMed:23387957, ECO:0000305}.
CC   -!- SUBUNIT: Interacts with host laminin and vitronectin. Can interact with
CC       both immobilized and soluble vitronectin. {ECO:0000269|PubMed:23230060,
CC       ECO:0000269|PubMed:23387957}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane. Cell surface.
CC   -!- DISRUPTION PHENOTYPE: Mutant displays a reduced binding to laminin,
CC       vitronectin, and epithelial cells, and is more sensitive to killing by
CC       human serum compared with the wild type. {ECO:0000269|PubMed:23230060,
CC       ECO:0000269|PubMed:23387957}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 9 family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAZF01000002; EDJ93357.1; -; Genomic_DNA.
DR   RefSeq; WP_005656358.1; NZ_AAZF01000002.1.
DR   AlphaFoldDB; A4N8V8; -.
DR   SMR; A4N8V8; -.
DR   EnsemblBacteria; EDJ93357; EDJ93357; CGSHi3655_02309.
DR   Proteomes; UP000003185; Unassembled WGS sequence.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   InterPro; IPR006129; AdhesinB.
DR   InterPro; IPR006128; Lipoprotein_4.
DR   InterPro; IPR006127; ZnuA-like.
DR   Pfam; PF01297; ZnuA; 1.
DR   PRINTS; PR00691; ADHESINB.
DR   PRINTS; PR00690; ADHESNFAMILY.
PE   1: Evidence at protein level;
KW   Cell outer membrane; Iron; Membrane; Metal-binding; Signal; Transport;
KW   Virulence.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..293
FT                   /note="Putative metal ABC transporter substrate-binding
FT                   protein Hpf"
FT                   /id="PRO_0000424420"
FT   REGION          23..48
FT                   /note="Interaction with host components"
FT   BINDING         58
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         123
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
FT   BINDING         189
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   293 AA;  32463 MW;  27FE3F9BACDFB508 CRC64;
     MRNSFKIMTA LALGLFAMQA NAKFKVVTTF TVIQDIAQNV AGNAATVESI TKPGAEIHEY
     EPTPKDIVKA QSADLILWNG LNLERWFERF FQNVKDKPAV VVTEGIQPLS IYEGPYKDAP
     NPHAWMSPSN ALIYIENIKN ALVKYDPQNA AVYEKNAADY AQKIKQLDEP LRAKLAQIPE
     AQRWLVTSEG AFSYLAKDYN LKEGYLWPIN AEQQGTPQQV RKVIDLVRKN NIPVVFSEST
     ISAKPAQQVA KESGAKYGGV LYVDSLSAKN GPVPTYIDLL NVTVSTIVKG FGK