PAPG1_ECOLX
ID PAPG1_ECOLX Reviewed; 335 AA.
AC P13720;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Fimbrial adhesin PapGI {ECO:0000303|PubMed:31361021};
DE Flags: Precursor;
GN Name=papGI {ECO:0000303|PubMed:31361021};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 700336 / J96 / UPEC;
RX PubMed=2886993; DOI=10.1073/pnas.84.16.5898;
RA Lund B., Lindberg F., Marklund B.-I., Normark S.;
RT "The PapG protein is the alpha-D-galactopyranosyl-(1-->4)-beta-D-
RT galactopyranose-binding adhesin of uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5898-5902(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700336 / J96 / UPEC;
RX PubMed=2895103; DOI=10.1128/jb.170.4.1887-1894.1988;
RA Lund B., Lindberg F., Normark S.;
RT "Structure and antigenic properties of the tip-located P pilus proteins of
RT uropathogenic Escherichia coli.";
RL J. Bacteriol. 170:1887-1894(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700336 / J96 / UPEC;
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).
RN [4]
RP PROTEIN SEQUENCE OF 22-39.
RX PubMed=2562836; DOI=10.1128/iai.57.1.76-81.1989;
RA Hoschuetzky H., Lottspeich F., Jann K.;
RT "Isolation and characterization of the alpha-galactosyl-1,4-beta-
RT galactosyl-specific adhesin (P adhesin) from fimbriated Escherichia coli.";
RL Infect. Immun. 57:76-81(1989).
RN [5]
RP FUNCTION.
RX PubMed=7885225; DOI=10.1111/j.1365-2958.1994.tb02175.x;
RA Haslam D.B., Boren T., Falk P., Ilver D., Chou A., Xu Z., Normark S.;
RT "The amino-terminal domain of the P-pilus adhesin determines receptor
RT specificity.";
RL Mol. Microbiol. 14:399-409(1994).
RN [6]
RP FUNCTION.
RX PubMed=31361021; DOI=10.1093/glycob/cwz059;
RA Legros N., Ptascheck S., Pohlentz G., Karch H., Dobrindt U., Muething J.;
RT "PapG subtype-specific binding characteristics of Escherichia coli towards
RT globo-series glycosphingolipids of human kidney and bladder uroepithelial
RT cells.";
RL Glycobiology 29:789-802(2019).
RN [7]
RP FUNCTION, SUBUNIT, DISULFIDE BOND, AND MUTAGENESIS OF 225-ASN--PRO-335;
RP 332-GLY--PHE-334 AND PHE-334.
RX PubMed=9351822; DOI=10.1093/emboj/16.21.6394;
RA Jones C.H., Danese P.N., Pinkner J.S., Silhavy T.J., Hultgren S.J.;
RT "The chaperone-assisted membrane release and folding pathway is sensed by
RT two signal transduction systems.";
RL EMBO J. 16:6394-6406(1997).
RN [8]
RP REVIEW.
RX PubMed=10049807; DOI=10.1006/jsbi.1998.4049;
RA Hung D.L., Hultgren S.J.;
RT "Pilus biogenesis via the chaperone/usher pathway: an integration of
RT structure and function.";
RL J. Struct. Biol. 124:201-220(1998).
CC -!- FUNCTION: Tip adhesin component of type P pili that binds
CC preferentially to host cell glycosphingolipids such as
CC globotriaosylceramide. {ECO:0000269|PubMed:2562836,
CC ECO:0000269|PubMed:2886993, ECO:0000269|PubMed:31361021,
CC ECO:0000269|PubMed:9351822}.
CC -!- SUBUNIT: Interacts with chaperone PapD. Assembly of the P pilus
CC requires periplasmic chaperone PapD, in absence of the chaperone
CC overexpression of this subunit is toxic, where the protein accumulates
CC in the periplasm. PapD stimulates release of PapG from an inner
CC membrane-associated form (where at least 1 disulfide bond can form)
CC into the periplasm and also helps it achieve its correct digalactoside-
CC binding conformation (PubMed:9351822). {ECO:0000269|PubMed:9351822}.
CC -!- INTERACTION:
CC P13720; P15319: papD; NbExp=2; IntAct=EBI-15725472, EBI-1034993;
CC -!- SUBCELLULAR LOCATION: Secreted. Fimbrium. Note=At the tip of P pili.
CC {ECO:0000269|PubMed:2886993}.
CC -!- PTM: Contains disulfide bonds (PubMed:9351822).
CC {ECO:0000269|PubMed:9351822}.
CC -!- SIMILARITY: Belongs to the adhesin PapG family. {ECO:0000305}.
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DR EMBL; M17317; AAA24285.1; -; Genomic_DNA.
DR EMBL; M20146; AAA24290.1; -; Genomic_DNA.
DR EMBL; X61239; CAA43570.1; -; Genomic_DNA.
DR PIR; G27743; G27743.
DR RefSeq; WP_000758676.1; NZ_POTA01000081.1.
DR AlphaFoldDB; P13720; -.
DR SMR; P13720; -.
DR DIP; DIP-60777N; -.
DR IntAct; P13720; 2.
DR PHI-base; PHI:7847; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0009289; C:pilus; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR CDD; cd00239; PapG_CBD; 1.
DR Gene3D; 2.60.40.1090; -; 1.
DR Gene3D; 2.60.40.1370; -; 1.
DR InterPro; IPR036937; Adhesion_dom_fimbrial_sf.
DR InterPro; IPR008966; Adhesion_dom_sf.
DR InterPro; IPR005310; PapG_carb-bd_N.
DR InterPro; IPR038420; PapG_carbohydrate-bd_sf.
DR InterPro; IPR005309; PapG_chaper-bd_C.
DR Pfam; PF03628; PapG_C; 1.
DR Pfam; PF03627; PapG_N; 1.
DR SUPFAM; SSF49401; SSF49401; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Direct protein sequencing; Disulfide bond; Fimbrium;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:2562836"
FT CHAIN 22..335
FT /note="Fimbrial adhesin PapGI"
FT /id="PRO_0000022005"
FT MUTAGEN 225..335
FT /note="Missing: No longer dependent on chaperone PapD for
FT release into periplasm."
FT /evidence="ECO:0000269|PubMed:9351822"
FT MUTAGEN 322..334
FT /note="GELSGSMTMVLSF->VELSGSMTMVLSS: No longer dependent on
FT chaperone PapD for release into periplasm."
FT /evidence="ECO:0000269|PubMed:9351822"
FT MUTAGEN 334
FT /note="F->S: Decreased dependence on chaperone PapD for
FT release into periplasm."
FT /evidence="ECO:0000269|PubMed:9351822"
SQ 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
