ID   AFAB_ECOLX              Reviewed;         247 AA.
AC   P53516;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Chaperone protein AfaB;
DE   Flags: Precursor;
GN   Name=afaB;
OS   Escherichia coli.
OG   Plasmid pIL1055.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A30 / UPEC;
RX   PubMed=8002584; DOI=10.1128/jb.176.24.7601-7613.1994;
RA   Garcia M.-I., Labigne A., le Bouguenec C.L.;
RT   "Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster
RT   and its translocation via flanking IS1 insertion sequences.";
RL   J. Bacteriol. 176:7601-7613(1994).
CC   -!- FUNCTION: Involved in the biogenesis of the AFA-III afimbrial adhesin.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone family.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-3 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA54116.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; X76688; CAA54115.1; -; Genomic_DNA.
DR   EMBL; X76688; CAA54116.1; ALT_INIT; Genomic_DNA.
DR   PIR; E55545; E55545.
DR   AlphaFoldDB; P53516; -.
DR   SMR; P53516; -.
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; Immunoglobulin domain; Periplasm; Plasmid; Signal.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..247
FT                   /note="Chaperone protein AfaB"
FT                   /id="PRO_0000009262"
SQ   SEQUENCE   247 AA;  26763 MW;  48F93B99950CA6EE CRC64;
     MKMRAVAVFT GMLTGVLSVA GLLSAGAYAA GGEGNMSASA TETNARVFSL HLGATRVVYN
     PASSGETLTV INDQDYPMLV QSEVLSEDQK SPAPFVVTPP LFRLDGQQSS RLRIVRTGGE
     FPPDRESLQW ICVKGIPPKE GDRWAEGKDG EKKADKVSLN VQLSVSSCIK LFVRPPAVKG
     RPDDVAGKVE WQRAGNRLKG VNPTPFYINL STLTVGGKEV KEREYIAPFS SREYPLPAGH
     RVRFSGR