#=GF ID SicP-binding
#=GF AC PF09119.14
#=GF DE SicP binding
#=GF AU Sammut SJ;0000-0003-4472-904X
#=GF SE pdb_1jyo
#=GF GA 25.00 25.00;
#=GF TC 26.40 29.80;
#=GF NC 24.70 20.90;
#=GF BM hmmbuild HMM.ann SEED.ann
#=GF SM hmmsearch -E 1000 -Z 75585367 --cpu 4 HMM pfamseq
#=GF TP Domain
#=GF RN [1]
#=GF RM 11689946
#=GF RT Maintenance of an unfolded polypeptide by a cognate chaperone in
#=GF RT bacterial type III secretion.
#=GF RA Stebbins CE, Galan JE;
#=GF RL Nature. 2001;414:77-81.
#=GF DR INTERPRO; IPR015203;
#=GF DR SCOP; 1jyo; fa;
#=GF DR SO; 0000417; polypeptide_domain;
#=GF CC Members of this family bind the chaperone SicP, which is
#=GF CC required both to maintain the stability of SptP, as well as to
#=GF CC ensure the eventual secretion of the protein. The domain is
#=GF CC found in the Salmonella effector protein SptP, which interacts
#=GF CC with SicP chaperone dimers mainly through four regions of its
#=GF CC chaperone-binding domain. The structure of the SptP-SicP complex
#=GF CC contains four molecules of SicP, aligned in a linear fashion and
#=GF CC arranged in two sets of tightly bound homodimers that bind two
#=GF CC SptP molecules. The SicP homodimers do not interact with each
#=GF CC other, but are held together by a molecular interface formed
#=GF CC between two SptP molecules. Each SptP molecule is wrapped around
#=GF CC by three SicP chaperones (two chaperones from one homodimer and
#=GF CC a third one from the opposite homodimer pair) [1].
#=GF SQ 11
#=GS A9MF96_SALAR/20-107 AC A9MF96.1
#=GS E3BEL0_9VIBR/32-115 AC E3BEL0.1
#=GS A0A2A2H945_9GAMM/1-79 AC A0A2A2H945.1
#=GS A0A0J6NKB8_9NEIS/33-116 AC A0A0J6NKB8.1
#=GS D2TY26_9GAMM/33-111 AC D2TY26.1
#=GS A0A261TTH2_9BORD/40-123 AC A0A261TTH2.1
#=GS BOPA_BURPS/31-114 AC Q63K42.1
#=GS SPTP_SALTY/41-121 AC P74873.1
#=GS A0A2X4T3S8_SALER/33-120 AC A0A2X4T3S8.1
#=GS A0A4Z0QAW5_SALET/41-121 AC A0A4Z0QAW5.1
#=GS A0A844TSB4_9BORD/49-141 AC A0A844TSB4.1
A9MF96_SALAR/20-107 ...APEKFASKVLTWLGRVPLFKNIDAVQKHMENTR.......VQNQKTLQVFLKALTEKYDEKSVNAITLMAGLND..SiKPFTPVRLQQI-----tqmvkdae
E3BEL0_9VIBR/32-115 ...AQFSFSDKVMHWLSQMPLLNNLAAVQEFAQKQT.......ESNLKTLGVFLNALAHERGEEYALKVANKMDYSG..Q.TPLTSRLIEHV-----tqgit...
A0A2A2H945_9GAMM/1-79 .ms----FNDHVLSTLAKLPFLKNENAIRTYVARLN.......ITAQQKLSVFLRSLAERYGLATAEQTLPRLDLSP..K.TPLTAHK---------iefipq..
A0A0J6NKB8_9NEIS/33-116 ...ASQGFKGRLYACLSQLPLLKNLEAVKSYSQRVQ.......AENQTALGVFINTLSHRYGQESAQAALDSMGRLQ..G.APLKQRVVEQLISVAE........
D2TY26_9GAMM/33-111 ...AQMSFNDHVLSTLAKLPFLKNENAIRTYVARLN.......ITVQQKLTVFLRSLAERYGLATTEQTLPKLDLSP..K.TPL-------------aahkiefi
A0A261TTH2_9BORD/40-123 ..a-QFTLNDRILYAFSYVPVLKYWEPVVTFTRDLE.......MKNAQVLGLFIHSLSTHYGSAKAEVAIRDLDLTG..A.TPLQSSTIERLIEIA-r.......
BOPA_BURPS/31-114 ...ARLGMKERLFAFLAHVPLLKHCDAVRRYAEQVR.......MENRRSLEVFVLALSKRYGPEGAKAAFDYGARRD..G.APLDQRRVRNMVSIAE........
SPTP_SALTY/41-121 ...APEKFSSKVLTWLGKMPLFKNTEVVQKHTENIR.......VQDQKILQTFLHALTEKYGETAVNDALLMSRINM..N.KPLTQRLA---VQITE........
A0A2X4T3S8_SALER/33-120 ...APEKFASKVLTWLGRVPLFKNIDAVQKHMENTR.......VQNQKTLQVFLKALTEKYDEKSVNAITLMAGLND..SiKPFTPVRVQQITQ---mvkdae..
A0A4Z0QAW5_SALET/41-121 ...APEKFSSKVLTWLGKMPLFKNTEVVQKHTENIK.......GQEQKILQTFLQALTEKYGETAVNNALLMSRINM..N.KPLTQRLA---VQITE........
A0A844TSB4_9BORD/49-141 aag---TFKGYVLAALSHIPIFRDLPAVVDYCNQLQsaeesalIENAQALGVFMHALAAKYGDRATERALMINDVSYdgH.TPLNARVVSRVIETAE........
#=GC seq_cons ...A..pFss+VLshLu+lPLhKNh-AVpcaspplp.......hpNQpsLpVFL+ALoc+YGppuspssl.hhclss..s.sPLst+hlpphhp...........
//
