ID L5KIX2_PTEAL Unreviewed; 748 AA.
AC L5KIX2;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Heat shock protein 75 kDa, mitochondrial {ECO:0000313|EMBL:ELK10721.1};
GN ORFNames=PAL_GLEAN10011622 {ECO:0000313|EMBL:ELK10721.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK10721.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; KB030715; ELK10721.1; -; Genomic_DNA.
DR AlphaFoldDB; L5KIX2; -.
DR STRING; 9402.L5KIX2; -.
DR eggNOG; KOG0019; Eukaryota.
DR InParanoid; L5KIX2; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR CDD; cd16927; HATPase_Hsp90-like; 1.
DR Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.40.50.11260; -; 1.
DR Gene3D; 1.20.120.790; Heat shock protein 90, C-terminal domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR HAMAP; MF_00505; HSP90; 1.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR037196; HSP90_C.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR Pfam; PF13589; HATPase_c_3; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF110942; HSP90 C-terminal domain; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW Stress response {ECO:0000313|EMBL:ELK10721.1}.
FT DOMAIN 152..305
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 85065 MW; C444A39A6EE7FD60 CRC64;
MPPRSLPTRR LRQRTGQPGA HRDVTHPRPG NAPPLVRAAA RALDTTDMAR ELRALLLWGR
RLRAPALAAA GAEKPILCLW RAPIQSICPR RNLASGFHVG RLFSSQAAED HQEALHSIIG
STETVQGSVS KHEFQAETKK LLDIVARSLY SEKEVFIREL ISNASDALEK LRHKLVSEGQ
TLPEMEIHLQ TDAEKGTITI QDTGIGMTQE ELVSNLGTIA RSGSKAFLDA LQNQAEASSK
IIGQFGVGFY SAFMVADRVK VYSRSASPGS PGYQWLSDGS GVFEIAEASG VRTGTKIIIH
LKSDCKEFAS EARVRDVVTK YSNFVSFPLY LNGKRINTLQ AVWMMDPKDV GEWQHEEFYR
YIAQAYDKPR YTLHYKTDAP LNIRSIFYVP EMKPSMFDVS RELGSSISLY SRKVLIQTKA
TDVLPKWLRF IRGVVDSEDI PLNLSRELLQ ESALIRKLRD VLQQRLIKFF VDQSKKDAEK
YAKFFEDYGL FMREGIVTTA EQEVKEDIAK LLRYESSALP AGQLTSLMDY ASRMQAGTRN
IYYLCAPSRH LAEHSPYYEA MKQKNMEVLF CYEQFDELTL LHLREFDKKK LISVETDIVV
DHYKEEKFED RSPADDRLSE KETEDLMAWM RNVLGSRVTN VKMTLRLDTH PAMITVLEMG
AARHFLRMQQ LAKTQEERAQ LLQPTLEINP RHILIKKLSQ LRESEADLAQ LLMEQIYENA
MIAAGLVDDP RPMVGRLNNL LVKALERH
//