ID A0A1H2ZBN7_9FLAO Unreviewed; 628 AA.
AC A0A1H2ZBN7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SDX14244.1};
GN ORFNames=SAMN04487892_3379 {ECO:0000313|EMBL:SDX14244.1};
OS Allomuricauda zhangzhouensis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Allomuricauda.
OX NCBI_TaxID=1073328 {ECO:0000313|EMBL:SDX14244.1, ECO:0000313|Proteomes:UP000199592};
RN [1] {ECO:0000313|Proteomes:UP000199592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25030 {ECO:0000313|Proteomes:UP000199592};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) 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; FNMY01000008; SDX14244.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2ZBN7; -.
DR STRING; 1073328.SAMN05216294_3384; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000199592; 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 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; 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.
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}.
FT DOMAIN 24..177
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 207..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 628 AA; 71927 MW; E440D5F86DCC437D CRC64;
MTTGKINVSV ENIFPLIKKF LYSDHEIFLR ELISNATDAT LKLKHLTSIG EAKVEYGNPM
IEVKVDKENK RIHIIDQGIG MTEDEVKKYI NEVAFSGAEE FLDKYKDAGK DSGIIGHFGL
GFYSAFMVAE KVEIISKSFK NEPAVHWTCD GSPEFSIEPH DKTERGTEIV LHVAEDSTEF
LEDAKIRELL VKYNKFMPIP IKFGTKTETL PKPEDAKEED PAPTQEVDNI INNPNPAWTK
QPTDLEDEDY KSFYRELYPM QFEEPLFHIH LNVDYPFNLT GILYFPKLTN DLNIQKDRIQ
LYQNQVFVTD NVEGIVPEFL TMLRGVIDSP DIPLNVSRSY LQADGAVKKI SSYITRKVAD
KLSSLFKNNR EDFEQKWNDI KVVIEYGMLS EDKFFEKADK FALYPTVDGK FYTFEELEAK
IKDNQTDKND KLVVLYASDK EAQHSYIDAA VAKGYEVLLM DSPIVSHLMQ KLETTKENLT
FARVDADHID NIIKKDEEAI SKLSDEEKDQ LKSELEKVTT DKGFTIQLEA MDSSASPFII
TEPEFMRRMK EMQQTGGGGM FGMGNIPDMY NLIVNTNHEL IGEILNTKTE KKRTRLINQS
LDLARLSKGL LKGEELTKFI SRSYEMIK
//
