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CSOA_ECOLX
ID   CSOA_ECOLX              Reviewed;         171 AA.
AC   P0ABW7; P25730;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 44.
DE   RecName: Full=CS1 fimbrial subunit A;
DE   AltName: Full=CS1 pilin;
DE   Flags: Precursor;
GN   Name=csoA; Synonyms=cooA;
OS   Escherichia coli.
OG   Plasmid pDEP23.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=O139:H28 / ETEC; PLASMID=pDEP23;
RX   PubMed=1679404; DOI=10.1016/0378-1097(91)90607-c;
RA   Jordi B.J.A.M., van Vliet A.H.M., Willshaw G.A., van der Zeijst B.A.M.,
RA   Gaastra W.;
RT   "Analysis of the first two genes of the CS1 fimbrial operon in human
RT   enterotoxigenic Escherichia coli of serotype 0139:H28.";
RL   FEMS Microbiol. Lett. 64:265-270(1991).
RN   [2]
RP   PROTEIN SEQUENCE OF 24-42.
RC   STRAIN=60R75;
RX   PubMed=2572583; DOI=10.1128/jb.171.11.6372-6374.1989;
RA   Hall R.H., Maneval D.R. Jr., Collins J.H., Theibert J.L., Levine M.M.;
RT   "Purification and analysis of colonization factor antigen I, coli surface
RT   antigen 1, and coli surface antigen 3 fimbriae from enterotoxigenic
RT   Escherichia coli.";
RL   J. Bacteriol. 171:6372-6374(1989).
CC   -!- FUNCTION: Fimbriae (also called pili), polar filaments radiating from
CC       the surface of the bacterium to a length of 0.5-1.5 micrometers and
CC       numbering 100-300 per cell, enable bacteria to colonize the epithelium
CC       of specific host organs.
CC   -!- SUBCELLULAR LOCATION: Fimbrium.
CC   -!- INDUCTION: CS1 fimbriae are only expressed in the presence of the
CC       positive regulator rns.
CC   -!- SIMILARITY: Belongs to the fimbrial CS1 protein family. {ECO:0000305}.
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DR   EMBL; X62879; CAA44673.1; -; Genomic_DNA.
DR   PIR; A41467; A41467.
DR   RefSeq; WP_000768757.1; NZ_LRLU01000168.1.
DR   RefSeq; YP_424820.1; NC_007635.1.
DR   PDB; 4HJI; X-ray; 1.60 A; A/B=35-171.
DR   PDBsum; 4HJI; -.
DR   AlphaFoldDB; P0ABW7; -.
DR   SMR; P0ABW7; -.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   InterPro; IPR007540; Fimbrial_CS1-type.
DR   Pfam; PF04449; Fimbrial_CS1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Direct protein sequencing; Fimbrium; Plasmid; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:2572583"
FT   CHAIN           24..171
FT                   /note="CS1 fimbrial subunit A"
FT                   /id="PRO_0000009180"
FT   CONFLICT        28
FT                   /note="I -> E (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          37..42
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          50..54
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          66..75
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          81..87
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          90..95
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          99..107
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          117..119
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   HELIX           121..124
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          127..129
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          132..134
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          138..144
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:4HJI"
FT   STRAND          156..169
FT                   /evidence="ECO:0007829|PDB:4HJI"
SQ   SEQUENCE   171 AA;  17542 MW;  46E70EE7053DBE13 CRC64;
     MKLKKTIGAM ALATLFATMG ASAVEKTISV TASVDPTVDL LQSDGSALPN SVALTYSPAV
     NNFEAHTINT VVHTNDSDKG VVVKLSADPV LSNVLNPTLQ IPVSVNFAGK PLSTTGITID
     SNDLNFASSG VNKVSSTQKL SIHADATRVT GGALTAGQYQ GLVSIILTKS T
 
 
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