ECPA_ECOL6
ID ECPA_ECOL6 Reviewed; 195 AA.
AC Q8CWB9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Common pilus major fimbrillin subunit EcpA;
DE AltName: Full=MatB fimbrillin;
DE Flags: Precursor;
GN Name=ecpA; Synonyms=matB; OrderedLocusNames=c0404;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 23-195, FUNCTION, SUBUNIT,
RP INTERACTION WITH ECPD, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-33;
RP LYS-68; ILE-91; LEU-98; 131-VAL-LEU-132; ALA-169 AND 169-ALA--THR-171.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=22355107; DOI=10.1073/pnas.1106733109;
RA Garnett J.A., Martinez-Santos V.I., Saldana Z., Pape T., Hawthorne W.,
RA Chan J., Simpson P.J., Cota E., Puente J.L., Giron J.A., Matthews S.;
RT "Structural insights into the biogenesis and biofilm formation by the
RT Escherichia coli common pilus.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3950-3955(2012).
CC -!- FUNCTION: Part of the ecpRABCDE operon, which encodes the E.coli common
CC pilus (ECP). ECP is found in both commensal and pathogenic strains and
CC plays a dual role in early-stage biofilm development and host cell
CC recognition. Major subunit of the fimbria.
CC {ECO:0000269|PubMed:22355107}.
CC -!- SUBUNIT: Self-associates. Forms filaments. Interacts with EcpD.
CC {ECO:0000269|PubMed:22355107}.
CC -!- SUBCELLULAR LOCATION: Fimbrium {ECO:0000269|PubMed:22355107}.
CC -!- INDUCTION: Negatively regulated by H-NS. Positively regulated by IHF
CC and EcpR (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the EcpA/MatB fimbrillin family. {ECO:0000305}.
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DR EMBL; AE014075; AAN78885.1; -; Genomic_DNA.
DR RefSeq; WP_000730985.1; NC_004431.1.
DR PDB; 3QS2; X-ray; 1.78 A; A/B=23-195.
DR PDB; 3QS3; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=41-195.
DR PDBsum; 3QS2; -.
DR PDBsum; 3QS3; -.
DR AlphaFoldDB; Q8CWB9; -.
DR SMR; Q8CWB9; -.
DR STRING; 199310.c0404; -.
DR EnsemblBacteria; AAN78885; AAN78885; c0404.
DR KEGG; ecc:c0404; -.
DR eggNOG; ENOG502Z9JQ; Bacteria.
DR HOGENOM; CLU_120328_0_0_6; -.
DR OMA; AQDQFTF; -.
DR BioCyc; ECOL199310:C0404-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.3290; -; 1.
DR InterPro; IPR016514; EcpA.
DR InterPro; IPR038478; Fimbrillin_EcpA_sf.
DR Pfam; PF16449; MatB; 1.
DR PIRSF; PIRSF007320; Fimbrillin_MatB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fimbrium; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..195
FT /note="Common pilus major fimbrillin subunit EcpA"
FT /id="PRO_0000367929"
FT MUTAGEN 33
FT /note="W->A: Mutant does not produce ECP and cannot form
FT biofilms."
FT /evidence="ECO:0000269|PubMed:22355107"
FT MUTAGEN 68
FT /note="K->E: Decreases ability to form biofilms."
FT /evidence="ECO:0000269|PubMed:22355107"
FT MUTAGEN 91
FT /note="I->A: Decreases ability to form biofilms; when
FT associated with D-98."
FT /evidence="ECO:0000269|PubMed:22355107"
FT MUTAGEN 98
FT /note="L->D: Decreases ability to form biofilms; when
FT associated with A-91."
FT /evidence="ECO:0000269|PubMed:22355107"
FT MUTAGEN 131..132
FT /note="VL->AA: Decreases ability to form biofilms."
FT /evidence="ECO:0000269|PubMed:22355107"
FT MUTAGEN 169..171
FT /note="AVT->DVD,WVW: Decreases ability to form biofilms."
FT /evidence="ECO:0000269|PubMed:22355107"
FT MUTAGEN 169
FT /note="A->W: Decreases ability to form biofilms."
FT /evidence="ECO:0000269|PubMed:22355107"
FT STRAND 25..40
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:3QS2"
FT TURN 59..62
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 67..76
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 83..92
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 104..111
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 122..126
FT /evidence="ECO:0007829|PDB:3QS2"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3QS2"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3QS2"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 145..171
FT /evidence="ECO:0007829|PDB:3QS2"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:3QS2"
FT STRAND 178..194
FT /evidence="ECO:0007829|PDB:3QS2"
SQ SEQUENCE 195 AA; 20111 MW; E07B06392F5CC43C CRC64;
MKKKVLAIAL VTVFTGTGVA QAADVTAQAV ATWSATAKKD TTSKLVVTPL GSLAFQYAEG
IKGFNSQKGL FDVAIEGDST ATAFKLTSRL ITNTLTQLDT SGSTLNVGVD YNGTAVEKTG
DTVMIDTANG VLGGNLSPLA NGYNASNRTT AQDGFTFSII SGTTNGTTAV TDYSTLPEGI
WSGDVSVQFD ATWTS
