6CD2


Conserved Protein Domain Family
PapG_C

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pfam03628: PapG_C 
PapG chaperone-binding domain
PapG, the adhesin of the P-pili, is situated at the tip and is only a minor component of the whole pilus structure. A two-domain structure has been postulated for PapG; a carbohydrate binding N-terminus and chaperone binding C-terminus (this domain). The chaperone-binding domain is highly conserved, and is essential for the correct assembly of the pili structure when aided by the chaperone molecule PapD.
Statistics
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PSSM-Id: 397609
Aligned: 4 rows
Threshold Bit Score: 198.202
Threshold Setting Gi: 75462967
Created: 11-May-2020
Updated: 7-Aug-2020
Structure
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Program:
Drawing:
Aligned Rows:
PubMed ReferencesClick to see Conserved Features Help

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
6CD2_B 208 HGDLSINSANNHYAAQTLSVSCDVPANIRFMLLRNTTPTYSHgKKFSVGLGHGWDSIVSVNGVDTGETTMRWYKAGTQNL 287
Q9AIQ1 229 HGNIVIDRANGNIASQTLSIYCDVPVSVKISLLRNTLPIYNN-NKFSVGLGNGWDSIISLDGVEQSEEILRWYTAGSKTV 307 Escherichia coli
Q9APE7 228 HGNLSIDSAHGNYASQAVTIYCDVPVTVKISLFSNTQPAYNN-QGVAVGLGNGWDSIIYLDGVKRNEETLRWNTAGSRTV 306 Escherichia coli
Q9L6E3 227 HGDLSINSANNHYAAQTLSVSCDVPTNIRFFLLSNTNPAYSHgQQFSVGLGHGWDSIVSINGVDTGETTMRWYRAGTQNL 306 Escherichia coli
6CD2_B 288 TIGSRLYGESSKIQPGVLSGSATLLMILP 316
Q9AIQ1 308 KIESRLYGEEGKRKPGELSGSMSMVLSFL 336 Escherichia coli
Q9APE7 307 TVGSKLYGEAGKITSGALSGSMTMIMHLP 335 Escherichia coli
Q9L6E3 307 TIGSRLYGESSKIQPGVLSGSATLLMILP 335 Escherichia coli
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