ID   SEFB_SALEN              Reviewed;         246 AA.
AC   P33387;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Chaperone protein SefB;
DE   Flags: Precursor;
GN   Name=sefB;
OS   Salmonella enteritidis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=149539;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=27655-3B;
RX   PubMed=8097515; DOI=10.1128/jb.175.9.2523-2533.1993;
RA   Clouthier S.C., Mueller K.-H., Doran J.L., Collinson S.K., Kay W.W.;
RT   "Characterization of three fimbrial genes, sefABC, of Salmonella
RT   enteritidis.";
RL   J. Bacteriol. 175:2523-2533(1993).
CC   -!- FUNCTION: Required for the biogenesis of the SefA (SEF14) fimbria.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the periplasmic pilus chaperone 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; L11009; AAA27220.1; -; Genomic_DNA.
DR   PIR; B40618; B40618.
DR   RefSeq; WP_001676217.1; NZ_WIAP01000020.1.
DR   AlphaFoldDB; P33387; -.
DR   SMR; P33387; -.
DR   PATRIC; fig|149539.321.peg.4621; -.
DR   OMA; LQWLCVK; -.
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; IPR018046; Pili_assmbl_chaperone_CS.
DR   InterPro; IPR016147; Pili_assmbl_chaperone_N.
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; Disulfide bond; Fimbrium biogenesis; Immunoglobulin domain;
KW   Periplasm; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..246
FT                   /note="Chaperone protein SefB"
FT                   /id="PRO_0000009289"
FT   DISULFID        124..155
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   246 AA;  28030 MW;  4E3CE4A65EAC4354 CRC64;
     MYILNKFIRR TVIFFFFCYL PIASSESKKI EQPLLTQKYY GLRLGTTRVI YKEDAPSTSF
     WIMNEKEYPI LVQTQVYNDD KSSKAPFIVT PPILKVESNA RTRLKVIPTS NLFNKNEESL
     YWLCVKGVPP LNDNESNNKN NITTNLNVNV VTNSCIKLIY RPKTIDLTTM EIADKLKLER
     KGNSIVIKNP TSSYVNIANI KSGNLSFNIP NGYIEPFGYA QLPGGVHSKI TLTILDDNGA
     EIIRDY