ID   CSGA_SALEN              Reviewed;         151 AA.
AC   P0A1E7; P55225;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 51.
DE   RecName: Full=Major curlin subunit;
DE   AltName: Full=Fimbrin SEF17;
DE   Flags: Precursor;
GN   Name=csgA; Synonyms=agfA;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-151.
RC   STRAIN=27655-3B;
RX   PubMed=8104955; DOI=10.1128/jcm.31.9.2263-2273.1993;
RA   Doran J.L., Collinson S.K., Burian J., Sarlos G., Todd E.C.D., Munro C.K.,
RA   Kay C.M., Banser P.A., Peterkin P.I., Kay W.W.;
RT   "DNA-based diagnostic tests for Salmonella species targeting agfA, the
RT   structural gene for thin, aggregative fimbriae.";
RL   J. Clin. Microbiol. 31:2263-2273(1993).
RN   [3]
RP   PROTEIN SEQUENCE OF 21-33.
RC   STRAIN=27655-3B;
RX   PubMed=1677357; DOI=10.1128/jb.173.15.4773-4781.1991;
RA   Collinson S.K., Emoedy L., Mueller K.-H., Trust T.J., Kay W.W.;
RT   "Purification and characterization of thin, aggregative fimbriae from
RT   Salmonella enteritidis.";
RL   J. Bacteriol. 173:4773-4781(1991).
RN   [4]
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   -!- 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; AAC43599.1; -; Genomic_DNA.
DR   PIR; JC6039; JC6039.
DR   RefSeq; WP_000771416.1; NZ_WIAP01000025.1.
DR   AlphaFoldDB; P0A1E7; -.
DR   GeneID; 66755549; -.
DR   PATRIC; fig|149539.316.peg.2052; -.
DR   OMA; NSEIQIY; -.
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; 4.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Fimbrium; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000269|PubMed:1677357"
FT   CHAIN           21..151
FT                   /note="Major curlin subunit"
FT                   /id="PRO_0000006371"
FT   CONFLICT        134..151
FT                   /note="SVMVRQVGFGNNATANQY -> DSYTQVAS (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   151 AA;  15305 MW;  B7DAC0D16B621359 CRC64;
     MKLLKVAAFA AIVVSGSALA GVVPQWGGGG NHNGGGNSSG PDSTLSIYQY GSANAALALQ
     SDARKSETTI TQSGYGNGAD VGQGADNSTI ELTQNGFRNN ATIDQWNAKN SDITVGQYGG
     NNAALVNQTA SDSSVMVRQV GFGNNATANQ Y