HSP71_CANAL
ID HSP71_CANAL Reviewed; 656 AA.
AC P41797; A0A1D8PFP4; Q5AKZ7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Heat shock protein SSA1;
GN Name=SSA1; Synonyms=HSP70; OrderedLocusNames=CAALFM_C113480WA;
GN ORFNames=CaO19.12447, CaO19.4980;
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 [MRNA].
RX PubMed=7558317; DOI=10.1128/iai.63.10.4039-4045.1995;
RA La Valle R., Bromuro C., Ranucci L., Muller H.M., Crisanti A., Cassone A.;
RT "Molecular cloning and expression of a 70-kilodalton heat shock protein of
RT Candida albicans.";
RL Infect. Immun. 63:4039-4045(1995).
RN [2]
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-244.
RX PubMed=7744244; DOI=10.1111/j.1574-6968.1995.tb07506.x;
RA Eroles P., Sentandreu M., Elorza M.V., Sentandreu R.;
RT "Cloning of a DNA fragment encoding part of a 70-kDa heat shock protein of
RT Candida albicans.";
RL FEMS Microbiol. Lett. 128:95-100(1995).
RN [6]
RP FUNCTION, INTERACTION WITH HUMAN HTN3, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS 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, ECO:0000269|PubMed:12761219}.
CC -!- SUBUNIT: Binds human HTN3/histatin-5, a peptide from saliva, and
CC mediates its fungicidal activity.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12761219}.
CC Secreted, cell wall {ECO:0000269|PubMed:12761219}.
CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S78163; AAB34280.1; -; mRNA.
DR EMBL; CP017623; AOW26952.1; -; Genomic_DNA.
DR EMBL; Z30210; CAA82929.1; -; mRNA.
DR PIR; S51712; S51712.
DR RefSeq; XP_722186.1; XM_717093.2.
DR AlphaFoldDB; P41797; -.
DR SMR; P41797; -.
DR BioGRID; 1219167; 9.
DR STRING; 237561.P41797; -.
DR COMPLUYEAST-2DPAGE; P41797; -.
DR PRIDE; P41797; -.
DR GeneID; 3636229; -.
DR KEGG; cal:CAALFM_C113480WA; -.
DR CGD; CAL0000184706; HSP70.
DR VEuPathDB; FungiDB:C1_13480W_A; -.
DR eggNOG; KOG0101; Eukaryota.
DR HOGENOM; CLU_005965_3_0_1; -.
DR InParanoid; P41797; -.
DR OMA; VVVQFKG; -.
DR OrthoDB; 288077at2759; -.
DR Reactome; R-HSA-6803157; Antimicrobial peptides.
DR PRO; PR:P41797; -.
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; IDA:CGD.
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:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:CGD.
DR GO; GO:0030445; C:yeast-form cell wall; 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:0051701; P:biological process involved in interaction with host; IDA:CGD.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
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:0044409; P:entry into host; IMP:CGD.
DR GO; GO:0044416; P:induction by symbiont of host defense response; IDA: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..656
FT /note="Heat shock protein SSA1"
FT /id="PRO_0000078364"
FT REGION 608..656
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250"
FT CONFLICT 176
FT /note="A -> G (in Ref. 5; AAB34280)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 70324 MW; 562BA08EDDFE2EFD CRC64;
MSKAVGIDLG TTYSCVAHFA NDRVEIIAND QGNRTTPSFV AFTDTERLIG DAAKNQAAMN
PANTVFDAKR LIGRKFDDPE VINDAKHFPF KVIDKAGKPV IQVEYKGETK TFSPEEISSM
VLTKMKEIAE GYLGSTVKDA VVTVPAYFND SQRQATKDAG TIAGLNVLRI INEPTAAAIA
YGLDKKGSRG EHNVLIFDLG GGTFDVSLLA IDEGIFEVKA TAGDTHLGGE DFDNRLVNFF
IQEFKRKNKK DISTNQRALR RLRTACERAK RTLSSSAQTS IEIDSLYEGI DFYTSITRAR
FEELCADLFR STLDPVGKVL ADAKIDKSQV EEIVLVGGST RIPKIQKLVS DFFNGKELNK
SINPDEAVAY GAAVQAAILT GDTSSKTQDI LLLDVAPLSL GIETAGGIMT KLIPRNSTIP
TKKSETFSTY ADNQPGVLIQ VFEGERAKTK DNNLLGKFEL SGIPPAPRGV PQIEVTFDID
ANGILNVSAL EKGTGKTQKI TITNDKGRLS KEEIDKMVSE AEKFKEEDEK EAARVQAKNQ
LESYAYSLKN TINDGEMKDK IGADDKEKLT KAIDETISWL DASQAASTEE YEDKRKELES
VANPIISGAY GAAGGAPGGA GGFPGAGGFP GGAPGAGGPG GATGGESSGP TVEEVD