ID   CSGB_SALEN              Reviewed;         151 AA.
AC   P0A1E9; P55226;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Minor curlin subunit;
DE   AltName: Full=Fimbrin SEF17 minor subunit;
DE   Flags: Precursor;
GN   Name=csgB; Synonyms=agfB;
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=8550497; DOI=10.1128/jb.178.3.662-667.1996;
RA   Collinson S.K., Clouthier S.C., Doran J.L., Banser P.A., Kay W.W.;
RT   "Salmonella enteritidis agfBAC operon encoding thin, aggregative
RT   fimbriae.";
RL   J. Bacteriol. 178:662-667(1996).
RN   [2]
RP   SUBCELLULAR LOCATION, INDUCTION, AND OPERON STRUCTURE.
RC   STRAIN=27655-3B;
RX   PubMed=17379722; DOI=10.1099/mic.0.2006/000935-0;
RA   Gibson D.L., White A.P., Rajotte C.M., Kay W.W.;
RT   "AgfC and AgfE facilitate extracellular thin aggregative fimbriae synthesis
RT   in Salmonella enteritidis.";
RL   Microbiology 153:1131-1140(2007).
CC   -!- FUNCTION: Curlin is the structural subunit of the curli. Curli are
CC       coiled surface structures that assemble preferentially at growth
CC       temperatures below 37 degrees Celsius. Curli can bind to fibronectin.
CC       The minor subunit is the nucleation component of curlin monomers.
CC   -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:17379722}. Note=Part
CC       of the curli surface structure.
CC   -!- INDUCTION: Constitutively expressed in agar-grown cells (at protein
CC       level), part of the csgBAC (agfBAC) operon.
CC       {ECO:0000269|PubMed:17379722}.
CC   -!- SIMILARITY: Belongs to the CsgA/CsgB family. {ECO:0000305}.
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DR   EMBL; U43280; AAC43598.1; -; Genomic_DNA.
DR   PIR; JC6040; JC6040.
DR   RefSeq; WP_000791655.1; NZ_WIAP01000025.1.
DR   AlphaFoldDB; P0A1E9; -.
DR   PRIDE; P0A1E9; -.
DR   PATRIC; fig|149539.316.peg.2053; -.
DR   OMA; INIVQGR; -.
DR   GO; GO:0009289; C:pilus; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   InterPro; IPR009742; Curlin_rpt.
DR   Pfam; PF07012; Curlin_rpt; 3.
PE   1: Evidence at protein level;
KW   Fimbrium; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..151
FT                   /note="Minor curlin subunit"
FT                   /id="PRO_0000006375"
SQ   SEQUENCE   151 AA;  16182 MW;  C0FC5430E6DD361D CRC64;
     MKNKLLFMML TILGAPGIAT ATNYDLARSE YNFAVNELSK SSFNQAAIIG QVGTDNSARV
     RQEGSKLLSV ISQEGGNNRA KVDQAGNYNF AYIEQTGNAN DASISQSAYG NSAAIIQKGS
     GNKANITQYG TQKTAVVVQK QSHMAIRVTQ R