ID   HIFB2_HAEIF             Reviewed;         241 AA.
AC   P45991;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=Chaperone protein HifB;
DE   Flags: Precursor;
GN   Name=hifB;
OS   Haemophilus influenzae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=727;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=86-0295 / LKP serotype 1;
RA   Green B.A., Olmsted S.B.;
RL   Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Mediates assembly of pili by forming soluble multimeric
CC       complexes with pili subunits as an intermediate step in the assembly
CC       process. This protein is involved in type B pili (HifA) assembly.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA61815.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; U19730; AAA61815.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; P45991; -.
DR   SMR; P45991; -.
DR   PRIDE; P45991; -.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   Gene3D; 2.60.40.10; -; 2.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR008962; PapD-like_sf.
DR   InterPro; IPR036316; Pili_assmbl_chap_C_dom_sf.
DR   InterPro; IPR001829; Pili_assmbl_chaperone_bac.
DR   InterPro; IPR016148; Pili_assmbl_chaperone_C.
DR   InterPro; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
DR   Pfam; PF02753; PapD_C; 1.
DR   Pfam; PF00345; PapD_N; 1.
DR   PRINTS; PR00969; CHAPERONPILI.
DR   SUPFAM; SSF49354; SSF49354; 1.
DR   SUPFAM; SSF49584; SSF49584; 1.
DR   PROSITE; PS00635; PILI_CHAPERONE; 1.
PE   3: Inferred from homology;
KW   Chaperone; Fimbrium biogenesis; Immunoglobulin domain; Periplasm; Signal.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..241
FT                   /note="Chaperone protein HifB"
FT                   /id="PRO_0000009280"
SQ   SEQUENCE   241 AA;  26718 MW;  8BB6854A42A220F8 CRC64;
     MGKTMFKKTL LFFTALFFAA LCAFSANADV IITGTRVIYP AGQKNVIVKL ENNDDSAALV
     QAWIDNGNPN ADPKYTKTPF VITPPVARVE AKSGQSLRIT FTGSEPLPDD RESLFYFNLL
     DIPPKPDAAF LAKHGSFMQI AIRSRLKLFY RPAKLSMDSR DAMKKVVFKA TPEGVLVDNQ
     TPYYMNYIGL LHQNKPAKNV KMVAPFSQAV FEAKGVRSGD KLKWVLVNDY GADQEGEAIA
     Q