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