ID A0A2K8SU94_9NOSO Unreviewed; 662 AA.
AC A0A2K8SU94;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=HtpG, molecular chaperone HtpG {ECO:0000313|EMBL:AUB38903.1};
GN ORFNames=COO91_04880 {ECO:0000313|EMBL:AUB38903.1};
OS Nostoc flagelliforme CCNUN1.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=2038116 {ECO:0000313|EMBL:AUB38903.1, ECO:0000313|Proteomes:UP000232003};
RN [1] {ECO:0000313|EMBL:AUB38903.1, ECO:0000313|Proteomes:UP000232003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCNUN1 {ECO:0000313|EMBL:AUB38903.1,
RC ECO:0000313|Proteomes:UP000232003};
RA Shang J.;
RT "Complete genome of a free-living desiccation-tolerant cyanobacterium and
RT its photosynthetic adaptation to extreme terrestrial habitat.";
RL Submitted (NOV-2017) 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; CP024785; AUB38903.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K8SU94; -.
DR KEGG; nfl:COO91_04880; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000232003; 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; 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.
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:UP000232003}.
FT DOMAIN 25..178
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 401..425
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 405..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 75460 MW; ED24C4D43123827F CRC64;
MLEQGTISIH TENIFPIIKK SLYSDHQIFL RELVSNAVDA IQKLKMVSRA GDYAGDIGEP
EIEIAIDKDK KTLSISDNGI GMTADEVKKY INQVAFSSAE EFIHKYEGKS DQPIIGHFGL
GFYSSFMVAQ KVEIDTLSYQ EGAQAVHWTC DGSPAFTLEE SPRTTRGTTI TLSLQGEEEE
FLESARIKNL VKTYCDFLPV PIKLEGEVLN KQKAPWRESP SNLSQEDYLE FYRYLYPFQE
EPLLWVHLNT DYPFIINGIL YFPKMRPDVD VTKGQIKLFC NQVFVSDNCE EIIPQFLTPM
RGVLDSTDIP LNVSRSALQG DRTVRRIGDY IAKKVGDRLK ELFRDNREQY ISAWKDLGTF
VKFGVLNDEK FKKQIEDIIV FRTTAKLTEK VAAETPVVEV QSSDGDAWQD VTPSPSSENS
APSAPYTTLK EYLERNKERN ENRVFYSTDE ATQATYIELH KNQGLEVLFM DSFIDTHFIN
FLEREYQDIK FTRVDSDLDN TLLEQDKATE IVDPKTNKTR SESIKELFEK SLNKPKLNIR
TEALKSDDPH GTPPAIVLLP EILRRMREMN AMMQQQSVEF PEDHVLLVNT AHPLIQNLAN
LNQGSIIQGD GQSPTDQLVN LICQHVYDLA LMSQKGFDAE GMKSFVERSN EVLTKLTEQA
SK
//
