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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
 
 
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