PRSJ_ECOLX
ID PRSJ_ECOLX Reviewed; 193 AA.
AC P42189;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Protein PrsJ;
DE Flags: Precursor;
GN Name=prsJ;
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: This protein maintains pilus integrity and thus is an
CC important participant in pilus assembly. It may function as molecular
CC chaperone directly or indirectly in the correct assembly of PapA
CC subunits.
CC -!- SUBCELLULAR LOCATION: Periplasm.
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DR EMBL; X62158; CAA44085.1; -; Genomic_DNA.
DR PIR; S25208; S25208.
DR AlphaFoldDB; P42189; -.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR InterPro; IPR029224; PapJ.
DR Pfam; PF14855; PapJ; 1.
PE 3: Inferred from homology;
KW Chaperone; Periplasm; Signal.
FT SIGNAL 1..27
FT /evidence="ECO:0000250"
FT CHAIN 28..193
FT /note="Protein PrsJ"
FT /id="PRO_0000022156"
SQ SEQUENCE 193 AA; 20836 MW; 44D1B31347354314 CRC64;
MVVNKTTAVL YLIALSLSGF IHTFLRAEER GIYDDVFTAD ELHHYRINER GGRTGSLAVS
GALLSSPCTL VSNEVPLSLR PENHSASRGA PLMLRLAGCG DGGALQPGKR GVAMTVSGSL
VTGPGSGSAL LPDRKLSGCD HLVIHDGDTF LLCRPDRRQE EMLAAWRKRA TQEGEYSDAR
SNPAMLRLSI KYE