ID K9WME9_9CYAN Unreviewed; 675 AA.
AC K9WME9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE SubName: Full=Molecular chaperone of HSP90 family {ECO:0000313|EMBL:AFZ20712.1};
GN ORFNames=Mic7113_5055 {ECO:0000313|EMBL:AFZ20712.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ20712.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ20712.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ20712.1,
RC ECO:0000313|Proteomes:UP000010471};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Chen A., Kyrpides N.,
RA Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL Submitted (JUN-2012) 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; CP003630; AFZ20712.1; -; Genomic_DNA.
DR RefSeq; WP_015184845.1; NC_019738.1.
DR AlphaFoldDB; K9WME9; -.
DR STRING; 1173027.Mic7113_5055; -.
DR KEGG; mic:Mic7113_5055; -.
DR PATRIC; fig|1173027.3.peg.5604; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_2_3; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000010471; 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; IPR003594; HATPase_C.
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; 2.
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.
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:UP000010471}.
FT DOMAIN 27..180
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 388..441
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..441
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 675 AA; 77169 MW; FBEEB14F322CA4A5 CRC64;
MTILEQGNIT IHTENIFPII KKSLYTDHEI FLRELISNSV DAIQKLKMVS YAGEVDGELE
EPEIVITIDK DNKTLSISDN GIGMTADEVK KYINQVAFSS AEEFIQKYQK DADQQIIGHF
GLGFYSSFMV AKKVEIDTLS YRAGAQAVHW SCDGSPAFEL TDSTRTQRGT TVTLTLQDEE
QEYIEAMRIK QLVKAYCDFM PVSIKLDGEQ INKQRALWKE SPQSLTTEDY LEFYRYLYPF
QEDPLLWVHL NTDYPFLLNG ILYFPKLKPD VDVTKGNIKL FCNQVFVSDH CEEVIPKFLM
PLRGVIDSPD IPLNVSRSAL TNDRTVRRIA DFIAKKVGDR LKSLYNEGRD EYIRCWQDVG
TFVKFGSLND DKFKKQVEDI IIYRTTHEAG EQGSKGTGEQ ASNPETPTVE VQSQEGDAWQ
EVTPSNTEDN PKSNTQKSTS NYTTLKEYLE RNKEHHENRV FYCNDEASQA TYVELHKNQG
LEVLFMDSFI DPHFISFLER EYSDVKFSRV DSDLDQTLID QDKEKEIVDP KTNKTRSEVI
KELFEKSLNK PKVNIKTQAL KSDDAQGTPP AMVLLPEAMR RLREMTALLQ QQNAEFPEEH
VLIVNTSHPL IENLYELSQG SIVQSSGQSP SGELANLICQ HVYDLALMAQ KGFDAEGMKS
FVERSNQVLT RLTQR
//
