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Fimbrial adhesin PapG

 PAPG_ECOLX              Reviewed;         335 AA.
P13720;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
01-JAN-1990, sequence version 1.
10-MAY-2017, entry version 80.
RecName: Full=Fimbrial adhesin PapG;
Flags: Precursor;
Name=papG;
Escherichia coli.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
STRAIN=ATCC 700336 / J96;
PubMed=2886993; DOI=10.1073/pnas.84.16.5898;
Lund B., Lindberg F., Marklund B.-I., Normark S.;
"The PapG protein is the alpha-D-galactopyranosyl-(1-->4)-beta-D-
galactopyranose-binding adhesin of uropathogenic Escherichia coli.";
Proc. Natl. Acad. Sci. U.S.A. 84:5898-5902(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 700336 / J96;
PubMed=2895103; DOI=10.1128/jb.170.4.1887-1894.1988;
Lund B., Lindberg F., Normark S.;
"Structure and antigenic properties of the tip-located P pilus
proteins of uropathogenic Escherichia coli.";
J. Bacteriol. 170:1887-1894(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 700336 / J96;
PubMed=1357526; DOI=10.1111/j.1365-2958.1992.tb01399.x;
Marklund B.-I., Tennent J.M., Garcia E., Hamers A., Baga M.,
Lindberg F., Gaastra W., Normark S.;
"Horizontal gene transfer of the Escherichia coli pap and prs pili
operons as a mechanism for the development of tissue-specific adhesive
properties.";
Mol. Microbiol. 6:2225-2242(1992).
[4]
PROTEIN SEQUENCE OF 22-39, AND FUNCTION.
PubMed=2562836;
Hoschuetzky H., Lottspeich F., Jann K.;
"Isolation and characterization of the alpha-galactosyl-1,4-beta-
galactosyl-specific adhesin (P adhesin) from fimbriated Escherichia
coli.";
Infect. Immun. 57:76-81(1989).
[5]
FUNCTION, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF
225-ASN--PRO-335; 332-GLY--PHE-334 AND PHE-334.
PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
"The chaperone-assisted membrane release and folding pathway is sensed
by two signal transduction systems.";
EMBO J. 16:6394-6406(1997).
[6]
REVIEW.
PubMed=10049807; DOI=10.1006/jsbi.1998.4049;
Hung D.L., Hultgren S.J.;
"Pilus biogenesis via the chaperone/usher pathway: an integration of
structure and function.";
J. Struct. Biol. 124:201-220(1998).
-!- FUNCTION: Binds the Gal-alpha(1-4)Gal receptor found on epithelial
cells lining the upper urinary tract (PubMed:2886993,
PubMed:2562836, PubMed:9351822). {ECO:0000269|PubMed:2562836,
ECO:0000269|PubMed:2886993, ECO:0000269|PubMed:9351822}.
-!- SUBUNIT: Interacts with chaperone PapD. Assembly of the P pilus
requires periplasmic chaperone PapD, in absence of the chaperone
overexpression of this subunit is toxic, where the protein
accumulates in the periplasm. PapD stimulates release of PapG from
an inner membrane-associated form (where at least 1 disulfide bond
can form) into the periplasm and also helps it achieve its correct
digalactoside-binding conformation (PubMed:9351822).
{ECO:0000269|PubMed:9351822}.
-!- SUBCELLULAR LOCATION: Secreted. Fimbrium. Note=At the tip of P
pili. {ECO:0000269|PubMed:2886993}.
-!- PTM: Contains disulfide bonds (PubMed:9351822).
{ECO:0000269|PubMed:9351822}.
-!- MISCELLANEOUS: Strains of E.coli that cause infection of the human
urinary tract produce pap-pili (P pili) which are hair-like
appendages consisting of about 1000 helically arranged subunits of
the protein PapA. These pili mediate binding to digalactoside-
containing glycolipids present on the epithelial cells which line
the urinary tract.
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EMBL; M17317; AAA24285.1; -; Genomic_DNA.
EMBL; M20146; AAA24290.1; -; Genomic_DNA.
EMBL; X61239; CAA43570.1; -; Genomic_DNA.
PIR; G27743; G27743.
RefSeq; WP_000758676.1; NZ_LJYA01000005.1.
ProteinModelPortal; P13720; -.
SMR; P13720; -.
DIP; DIP-60777N; -.
PRIDE; P13720; -.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
CDD; cd00239; PapG_CBD; 1.
InterPro; IPR008966; Adhesion_dom.
InterPro; IPR005310; PapG_carb-bd_N.
InterPro; IPR005309; PapG_chaper-bd_C.
Pfam; PF03628; PapG_C; 1.
Pfam; PF03627; PapG_N; 1.
ProDom; PD484789; PapG_chaper_bd_C; 1.
SUPFAM; SSF49401; SSF49401; 1.
1: Evidence at protein level;
Cell adhesion; Direct protein sequencing; Disulfide bond; Fimbrium;
Secreted; Signal.
SIGNAL 1 21 {ECO:0000269|PubMed:2562836}.
CHAIN 22 335 Fimbrial adhesin PapG.
/FTId=PRO_0000022005.
MUTAGEN 225 335 Missing: No longer dependent on chaperone
PapD for release into periplasm.
{ECO:0000269|PubMed:9351822}.
MUTAGEN 322 334 GELSGSMTMVLSF->VELSGSMTMVLSS: No longer
dependent on chaperone PapD for release
into periplasm.
{ECO:0000269|PubMed:9351822}.
MUTAGEN 334 334 F->S: Decreased dependence on chaperone
PapD for release into periplasm.
{ECO:0000269|PubMed:9351822}.
SEQUENCE 335 AA; 38281 MW; 4C3392586676E939 CRC64;
MKKWFPAFLF LSLSGGNDAL AGWHNVMFYA FNDYLTTNAG NVKVIDQPQL YIPWNTGSAT
ATYYSCSGPE FASGVYFQEY LAWMVVPKHV YTNEGFNIFL DVQSKYGWSM ENENDKDFYF
FVNGYEWDTW TNNGARICFY PGNMKQLNNK FNDLVFRVLL PVDLPKGHYN FPVRYIRGIQ
HHYYDLWQDH YKMPYDQIKQ LPATNTLMLS FDNVGGCQPS TQVLNIDHGS IVIDRANGNI
ASQTLSIYCD VPVSVKISLL RNTPPIYNNN KFSVGLGNGW DSIISLDGVE QSEEILRWYT
AGSKTVKIES RLYGEEGKRK PGELSGSMTM VLSFP


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