Protein Information

General Information
MoonProt ID405
First appeared in release3.0
Name(s)heat shock protein SSA1, gene: SSA1, HSP70
UniProt IDP41797
GO termsGO:0044416 induction by symbiont of host defense response P GO:0042277 peptide binding F GO:0005829 cytosol C GO:0005886 plasma membrane C GO:0030445 yeast-form cell wall C GO:0030446 hyphal cell wall C GO:0051701 interaction with host P GO:0009986 cell surface C GO:0009277 fungal-type cell wall C GO:0009636 response to toxic substance P GO:0034605 cellular response to heat P GO:0062040 fungal biofilm matrix C GO:0044409 entry into host P GO:0016192 vesicle-mediated transport P GO:0006986 response to unfolded protein P GO:0005829 cytosol C GO:0051787 misfolded protein binding F GO:0051085 chaperone cofactor-dependent protein refolding P GO:0051082 unfolded protein binding F GO:0042026 protein refolding P GO:0034620 cellular response to unfolded protein P GO:0031072 heat shock protein binding F GO:0016887 ATPase activity F GO:0006616 SRP-dependent cotranslational protein targeting to membrane, translocation P GO:0005886 plasma membrane C GO:0005737 cytoplasm C GO:0005634 nucleus C GO:0005524 ATP binding F GO:0044183 protein folding chaperone F GO:0005576 extracellular region C GO:0005524 ATP binding F GO:0005618 cell wall C GO:0000166 nucleotide binding F GO:0005737 cytoplasm C GO:0005886 plasma membrane C GO:0019730 antimicrobial humoral response P GO:0005737 cytoplasm C GO:0005618 cell wall C
Organisms for which functions have been demonstratedCandida albicans (yeast, a fungi, can cause candiadiasis)
Sequence length656 amino acids
FASTA sequence>sp|P41797|HSP71_CANAL Heat shock protein SSA1 OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=SSA1 PE=1 SV=2 MSKAVGIDLGTTYSCVAHFANDRVEIIANDQGNRTTPSFVAFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRKFDDPEVINDAKHFPFKVIDKAGKPVIQVEYKGETKTFSPEEISSMVLTKMKEIAEGYLGSTVKDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGSRGEHNVLIFDLGGGTFDVSLLAIDEGIFEVKATAGDTHLGGEDFDNRLVNFFIQEFKRKNKKDISTNQRALRRLRTACERAKRTLSSSAQTSIEIDSLYEGIDFYTSITRARFEELCADLFRSTLDPVGKVLADAKIDKSQVEEIVLVGGSTRIPKIQKLVSDFFNGKELNKSINPDEAVAYGAAVQAAILTGDTSSKTQDILLLDVAPLSLGIETAGGIMTKLIPRNSTIPTKKSETFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIDKMVSEAEKFKEEDEKEAARVQAKNQLESYAYSLKNTINDGEMKDKIGADDKEKLTKAIDETISWLDASQAASTEEYEDKRKELESVANPIISGAYGAAGGAPGGAGGFPGAGGFPGGAPGAGGPGGATGGESSGPTVEEVD
Structure Information
PDB IDNA
Quaternary structureNA
SCOPNA
CATHNA
TM Helix Predictionno TM helices
DisProt AnnotationNot in DisProt
Predicted Disorder RegionsUse FASTA sequence on the MFDp2 webserver. moonID_405_uniID_P41797 is 656 residues long, with 167 residues (25.46%) predicted as disordered.The protein has 0 short (< 30 residues) disorder segments and 1 long (>= 30 residues) disorder segment. Segment 1 - Long (>= 30 residues) disordered segment Segment is located between positions 490 and 656 in the sequence. The segment is 167 residues long (25.46 % of the total sequence length).
Connections to Disease
OMIM ID
Function 1
Function descriptionchaperone protein, intracellular function
References for functionSun, J.N.; Solis, N.V.; Phan, Q.T.; Bajwa, J.S.; Kashleva, H.; Thompson, A.; Liu, Y.; Dongari-Bagtzoglou, A.; Edgerton, M.; Filler, S.G. Host cell invasion and virulence mediated by Candida albicans Ssa1. PLoS Pathog. 2010, 6, e1001181. Li, X.S.; Reddy, M.S.; Baev, D.; Edgerton, M. Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5. J. Biol. Chem. 2003, 278, 28553–28561.
E.C. numberNA
Location of functional site(s)NA
Cellular location of functionintracellular
CommentsNA
Function 2
Function descriptioninducing endocytosis, belongs to heat shock protein 70 (Hsp 70) family
References for functionLi, X.S.; Reddy, M.S.; Baev, D.; Edgerton, M. Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5. J. Biol. Chem. 2003, 278, 28553–28561.
E.C. numberNA
Location of functional site(s)NA
Cellular location of functionreported to be at the yeast cell wall
Commentslatex beads were rapidly endocytosed by oral epithelial and endothelial cells, suggesting its role in virulence