ID H1Y0B2_9SPHI Unreviewed; 627 AA.
AC H1Y0B2;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE SubName: Full=Heat shock protein Hsp90 {ECO:0000313|EMBL:EHQ28161.1};
GN ORFNames=Mucpa_4070 {ECO:0000313|EMBL:EHQ28161.1};
OS Mucilaginibacter paludis DSM 18603.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=714943 {ECO:0000313|EMBL:EHQ28161.1, ECO:0000313|Proteomes:UP000002774};
RN [1] {ECO:0000313|EMBL:EHQ28161.1, ECO:0000313|Proteomes:UP000002774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18603 {ECO:0000313|EMBL:EHQ28161.1,
RC ECO:0000313|Proteomes:UP000002774};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Held B.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The permanent draft genome of Mucilaginibacter paludis DSM 18603.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; CM001403; EHQ28161.1; -; Genomic_DNA.
DR RefSeq; WP_008508910.1; NZ_CM001403.1.
DR AlphaFoldDB; H1Y0B2; -.
DR STRING; 714943.Mucpa_4070; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_10; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000002774; Chromosome.
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 InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR019805; Heat_shock_protein_90_CS.
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:SF97; ENDOPLASMIN; 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 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.
DR PROSITE; PS00298; HSP90; 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:UP000002774};
KW Stress response {ECO:0000313|EMBL:EHQ28161.1}.
SQ SEQUENCE 627 AA; 71416 MW; 1C08CA54C1F38AD7 CRC64;
MQEKGTISIH TENIFPIIKK FLYSDHEIFL RELVSNAVDA TQKIKRLASL GQYNGELGDL
KVEVAFDEAA KTITISDNGL GMTAEEIKKY INQIAFSGAT EFMEKFKDAK DANEIIGRFG
LGFYSAFMVA DQVEIQTLSY QDGAEPARWV CDGSTEFEIT EGSRTTRGTD IIMHINADGE
EFLDKNRIQG ILDKYCKFLP VPIKFGTQTD REQDGEDEEG KPKYTEVETD NIINNTNPIW
TKAPSELIDQ DYLDFYKELY PFSEDPLFWI HLNVDYPFNL TGVLYFPKVK NDFEIQKNKI
KLYSRQVFIT DEVKDIVPEF LMLLHGVIDS PDIPLNVSRS FLQADGNVKK INNYITKKVA
DKLAELFKSD RKSFEEKWSD IGLFVKYGMI SEDKFYDKAK DFALLTNTKQ EFFTLEEYKA
KVTPNQTDKD GTTVYLYTND PAKQDTFIQS ANKKDYDVLL MNSPIDNHFV AQLEQKLEKT
SVKRVDADVI DKLIKKEDAP AHVLTEEQSA KIKTIFDKAV AKANFKVEIE SLNPDELPVT
VTMDEFMRRM KDMAAMGGGM SFYGSMPDNY KVSINGNHKL ISRIAQAESE EEQTQLAKQA
FDLALLSQGM LTGPELTEFV NRSVSLI
//
