HSP72_CANAL
ID HSP72_CANAL Reviewed; 645 AA.
AC P46587; A0A1D8PD89; Q59VM8;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 4.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Heat shock protein SSA2;
GN Name=SSA2; Synonyms=SSA1; OrderedLocusNames=CAALFM_C104300CA;
GN ORFNames=CaO19.1065, CaO19.8667;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 453-645, AND SUBCELLULAR LOCATION.
RC STRAIN=3153A;
RX PubMed=8757872; DOI=10.1128/iai.64.8.3333-3340.1996;
RA Lopez-Ribot J.L., Alloush H.M., Masten B.J., Chaffin W.L.;
RT "Evidence for presence in the cell wall of Candida albicans of a protein
RT related to the hsp70 family.";
RL Infect. Immun. 64:3333-3340(1996).
RN [5]
RP FUNCTION, INTERACTION WITH HUMAN HTN3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12761219; DOI=10.1074/jbc.m300680200;
RA Li X.S., Reddy M.S., Baev D., Edgerton M.;
RT "Candida albicans Ssa1/2p is the cell envelope binding protein for human
RT salivary histatin 5.";
RL J. Biol. Chem. 278:28553-28561(2003).
CC -!- FUNCTION: May play a role in the transport of polypeptides both across
CC the mitochondrial membranes and into the endoplasmic reticulum.
CC {ECO:0000250}.
CC -!- FUNCTION: Binds HTN3/histatin-5, a peptide from human saliva, and
CC mediates its fungicidal activity. {ECO:0000269|PubMed:12761219}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8757872}. Secreted,
CC cell wall {ECO:0000269|PubMed:8757872}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR EMBL; CP017623; AOW26104.1; -; Genomic_DNA.
DR EMBL; U25718; AAC49388.1; -; mRNA.
DR RefSeq; XP_713669.2; XM_708576.2.
DR AlphaFoldDB; P46587; -.
DR SMR; P46587; -.
DR BioGRID; 1227747; 8.
DR STRING; 237561.P46587; -.
DR ChEMBL; CHEMBL1255136; -.
DR PRIDE; P46587; -.
DR GeneID; 3644711; -.
DR KEGG; cal:CAALFM_C104300CA; -.
DR CGD; CAL0000184853; SSA2.
DR VEuPathDB; FungiDB:C1_04300C_A; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_2_1; -.
DR InParanoid; P46587; -.
DR OrthoDB; 288077at2759; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR PRO; PR:P46587; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0009986; C:cell surface; IDA:CGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0062040; C:fungal biofilm matrix; IDA:CGD.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CGD.
DR GO; GO:0030446; C:hyphal cell wall; IDA:CGD.
DR GO; GO:0016020; C:membrane; IDA:CGD.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0031072; F:heat shock protein binding; IBA:GO_Central.
DR GO; GO:0051787; F:misfolded protein binding; IBA:GO_Central.
DR GO; GO:0042277; F:peptide binding; IDA:CGD.
DR GO; GO:0044183; F:protein folding chaperone; IBA:GO_Central.
DR GO; GO:0051082; F:unfolded protein binding; IBA:GO_Central.
DR GO; GO:0034620; P:cellular response to unfolded protein; IBA:GO_Central.
DR GO; GO:0051085; P:chaperone cofactor-dependent protein refolding; IBA:GO_Central.
DR GO; GO:0015833; P:peptide transport; IMP:CGD.
DR GO; GO:0042026; P:protein refolding; IBA:GO_Central.
DR GO; GO:0009636; P:response to toxic substance; IMP:CGD.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 1.20.1270.10; -; 1.
DR Gene3D; 2.60.34.10; -; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018181; Heat_shock_70_CS.
DR InterPro; IPR029048; HSP70_C_sf.
DR InterPro; IPR029047; HSP70_peptide-bd_sf.
DR InterPro; IPR013126; Hsp_70_fam.
DR PANTHER; PTHR19375; PTHR19375; 1.
DR Pfam; PF00012; HSP70; 1.
DR SUPFAM; SSF100920; SSF100920; 1.
DR SUPFAM; SSF100934; SSF100934; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00297; HSP70_1; 1.
DR PROSITE; PS00329; HSP70_2; 1.
DR PROSITE; PS01036; HSP70_3; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cell wall; Cytoplasm; Nucleotide-binding;
KW Reference proteome; Secreted; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..645
FT /note="Heat shock protein SSA2"
FT /id="PRO_0000078365"
FT REGION 581..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT CONFLICT 577..581
FT /note="SWLDA -> AWLDS (in Ref. 4; AAC49388)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 645 AA; 70071 MW; 063BD314C9755686 CRC64;
MSKAVGIDLG TTYSCVAHFA NDRVEIIAND QGNRTTPSFV AFTDTERLIG DAAKNQAAMN
PANTVFDAKR LIGRKFDDHE VQGDIKHFPF KVVDKASKPM IQVEYKGETK TFSPEEISSM
ILGKMKETAE GFLGTTVKDA VVTVPAYFND SQRQATKDAG TIAGLNVMRI INEPTAAAIA
YGLDKKSEAE KNVLIFDLGG GTFDVSLLSI EDGIFEVKAT AGDTHLGGED FDNRLVNFFI
QEFKRKNKKD ISTNQRALRR LRTACERAKR TLSSSAQTSI EIDSLYEGID FYTSITRARF
EELCADLFRS TLEPVDKVLS DAKIDKSKVD EIVLVGGSTR IPKVQKLVSD YFNGKEPNRS
INPDEAVAYG AAVQAAILSG DTSSKTQDLL LLDVAPLSLG IETAGGIMTK LIPRNSTIPT
KKSETFSTYA DNQPGVLIQV FEGERAQTKD NNLLGKFELS GIPPAPRGVP QIEVTFDIDA
NGILNVSALE KGTGKTQKIT ITNDKGRLSK EEIEKMVSEA EKFKEEDEKE ASRVQAKNQL
ESYAYSLKNT LGEEQFKSKL DASEIEEVTK AADETISWLD ANQTATQEEF ADQQKELESK
ANPIMTKAYQ AGATPSGAAG AAPGGFPGGA APEPSNDGPT VEEVD
