ID A0A367Y4V9_9MICO Unreviewed; 613 AA.
AC A0A367Y4V9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=HSP90 family protein {ECO:0000313|EMBL:RCK60092.1};
GN ORFNames=DTO57_08140 {ECO:0000313|EMBL:RCK60092.1};
OS Microbacterium sorbitolivorans.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=1867410 {ECO:0000313|EMBL:RCK60092.1, ECO:0000313|Proteomes:UP000253508};
RN [1] {ECO:0000313|EMBL:RCK60092.1, ECO:0000313|Proteomes:UP000253508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C1.15228 {ECO:0000313|EMBL:RCK60092.1,
RC ECO:0000313|Proteomes:UP000253508};
RA An D.;
RT "Microbacterium endoborsara sp. nov., a novel actinobacterium isolated from
RT Borszczowia aralocaspica.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RCK60092.1}.
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DR EMBL; QORO01000002; RCK60092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367Y4V9; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000253508; 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 Gene3D; 3.30.230.80; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR001404; Hsp90_fam.
DR InterPro; IPR020575; Hsp90_N.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR PANTHER; PTHR11528:SF26; HEAT SHOCK PROTEIN (HSP90 FAMILY)-RELATED; 1.
DR PANTHER; PTHR11528; HEAT SHOCK PROTEIN 90 FAMILY MEMBER; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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:UP000253508}.
SQ SEQUENCE 613 AA; 66823 MW; 05116D896D69B95E CRC64;
MTDTTARPFQ VDLRGVVDLL GRHIYSSPQV FLRELLQNGR DAIRARHDLD PSAPAGTLDI
VPAGPGEFRF RDDGVGLTAD EAAELLSTVG RSSKRDDVLG ERREGYLGQF GIGLLSCFMV
SDRIHVTSRS AKGAPAIEWV GDASGEFRIR ELGEAETAAL PIGTEIVLAP RPDDAAMLAR
EQVTALADHF GRYLPVAVRV QEETGSWRRV SREPEFLTDD REQLLAFGEQ VLGARPLDAI
RLNIEGTATR GVAYVLPYAP PPGARQANTV YLGRMLVSEH VDDMLPEWAF FVRAVLDTTG
LAPTASRESF VDSPALEHTR EEIGSAVRAW ILEQARAKPW VFQRFLGVHH LALKAMTLGD
DEFARTVLPW LPVETSAGDM TIGELAERYG GARYTESVDE FRQIAAVARD GYPVVNGGYV
HQAAIMRRLP VLLDLPVSRA SVNDILDDLA PVPLDDRARA VDLETRATTA LADVGCAVTT
RQFAPEELPA LVVVDPEVQR RIDREQVKGD IGGGLWGGIV GSVGDLIDKR RSADPAAAQA
AQLCLNWRSP LVKRLAHLGD ELVLSRTVRL LYVQALLASQ RPLQANDRRI LTQALGDMVS
LSAGFTDHEG GAL
//