#=GF ID PapG_C
#=GF AC PF03628.17
#=GF DE PapG chaperone-binding domain
#=GF AU Finn RD;0000-0001-8626-2148
#=GF SE Pfam-B_3074 (release 7.0)
#=GF GA 20.00 20.00;
#=GF TC 20.00 20.70;
#=GF NC 19.30 19.00;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch --cpu 4 -Z 75585367 -E 1000 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 11454740
#=GF RT The solution structure of PapGII from uropathogenic Escherichia
#=GF RT coli and its recognition of glycolipid receptors.
#=GF RA Sung MA, Fleming K, Chen HA, Matthews S;
#=GF RL EMBO Rep 2001;2:621-627.
#=GF RN [2]
#=GF RM 11440716
#=GF RT Structural basis of the interaction of the pyelonephritic E.
#=GF RT coli adhesin to its human kidney receptor.
#=GF RA Dodson KW, Pinkner JS, Rose T, Magnusson G, Hultgren SJ, Waksman
#=GF RA G;
#=GF RL Cell 2001;105:733-743.
#=GF DR INTERPRO; IPR005309;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC PapG, the adhesin of the P-pili, is situated at the tip and is
#=GF CC only a minor component of the whole pilus structure. A
#=GF CC two-domain structure has been postulated for PapG; a
#=GF CC carbohydrate binding N-terminus and chaperone binding
#=GF CC C-terminus (this domain). The chaperone-binding domain is highly
#=GF CC conserved, and is essential for the correct assembly of the
#=GF CC pili structure when aided by the chaperone molecule PapD [1,2].
#=GF SQ 2
#=GS A0A1B7JWF5_9GAMM/231-335 AC A0A1B7JWF5.1
#=GS A0A1G7HMJ9_9BACT/41-122 AC A0A1G7HMJ9.1
A0A1B7JWF5_9GAMM/231-335 .........fg--ALPMSVADTASKSLSMNVSCVSPGNIKVTYQ--PSNAYDA..aNPTRTDLGLGWYGELAM.NGSKR--TTMTFNNMTSQNVQIDVNLGKKVANPSAGNINGGGVLVF---eyi.....
A0A1G7HMJ9_9BACT/41-122 tmslpmsgpen----------------------------------ATRPTYEHgklMRFVRSSSNGWANNISItDAVTQKTTSLRFWPAKVQNMTIVAVSYGEDQKLS---------------vsahtmtp
#=GC seq_cons ..........s...................................spssY-t..h..hhps.u.GWhspluh.suspp..TohpF.shpsQNhpIsss.htcstp.S.................h.....
//