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PRSH_ECOLX
ID   PRSH_ECOLX              Reviewed;         195 AA.
AC   P42185;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=PRS fimbrial minor pilin protein;
DE   Flags: Precursor;
GN   Name=prsH;
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1442;
RX   PubMed=1357526; DOI=10.1111/j.1365-2958.1992.tb01399.x;
RA   Marklund B.-I., Tennent J.M., Garcia E., Hamers A., Baga M., Lindberg F.,
RA   Gaastra W., Normark S.;
RT   "Horizontal gene transfer of the Escherichia coli pap and prs pili operons
RT   as a mechanism for the development of tissue-specific adhesive
RT   properties.";
RL   Mol. Microbiol. 6:2225-2242(1992).
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   -!- FUNCTION: Seems to anchor the pilus to the bacterial cell. In addition
CC       the stoichiometric relationship between PrsH and PrsA determines the
CC       pilus length.
CC   -!- SUBCELLULAR LOCATION: Secreted. Fimbrium.
CC   -!- SIMILARITY: Belongs to the fimbrial protein family. {ECO:0000305}.
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DR   EMBL; X62157; CAA44082.1; -; Genomic_DNA.
DR   PIR; S25205; S25205.
DR   RefSeq; WP_021528975.1; NZ_UCUV01000013.1.
DR   AlphaFoldDB; P42185; -.
DR   SMR; P42185; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR   GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR   Gene3D; 2.60.40.1090; -; 1.
DR   InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR   InterPro; IPR008966; Adhesion_dom_sf.
DR   SUPFAM; SSF49401; SSF49401; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Fimbrium; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000250"
FT   CHAIN           23..195
FT                   /note="PRS fimbrial minor pilin protein"
FT                   /id="PRO_0000009199"
FT   DISULFID        58..97
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   195 AA;  21837 MW;  A5065E8F93D5861B CRC64;
     MRLRFSVPLF FFGCVFVHGV FAGPFPPPGM SLPEYWGEEH VWWDGRATFH GEVVRPACTL
     AMEDAWQIID MGETPVRDLQ NGFSGPERKF SLRLRNCEFN SQGGNLFSDS RIRVTFDGVR
     GETPDKFNLS GQAKGINLQI ADARGNIARA GKVMPAIPLT GNEEALDYTL RIVRNGKKLE
     AGNYFAVLGF RVDYE
 
 
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