ID A0A2G3J7P5_9NEIS Unreviewed; 633 AA.
AC A0A2G3J7P5;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chaperone protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000256|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000256|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000256|HAMAP-Rule:MF_00505};
GN ORFNames=CSQ88_16910 {ECO:0000313|EMBL:PHV00508.1};
OS Iodobacter sp. BJB302.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Iodobacter.
OX NCBI_TaxID=1506510 {ECO:0000313|EMBL:PHV00508.1, ECO:0000313|Proteomes:UP000224670};
RN [1] {ECO:0000313|EMBL:PHV00508.1, ECO:0000313|Proteomes:UP000224670}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BJB302 {ECO:0000313|EMBL:PHV00508.1,
RC ECO:0000313|Proteomes:UP000224670};
RA Jude B.A., Perron G.P., O'Brien K., Doing G., Bettina A.M.;
RT "Draft genomes of phenotypically distinct violacein producing isolates
RT cultured from the Hudson Valley Watershed.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000256|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239, ECO:0000256|HAMAP-Rule:MF_00505}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00505}.
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:PHV00508.1}.
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DR EMBL; PDZG01000060; PHV00508.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G3J7P5; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000224670; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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 HAMAP; MF_00505; HSP90; 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, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00505};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 26..181
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..337
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 559..633
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT COILED 495..524
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 633 AA; 71088 MW; AF8E4A12F2DFEBF1 CRC64;
MAKETLGFQT EVKQLLQLMI HSLYSNKEIF LRELISNASD ACDKLRFEAL NDASLYGEDS
ELKISLSFDK EARTLTLSDN GIGMSRDEVV KNIGTIARSG TKEFFGKLSG DAQKDANLIG
QFGVGFYSAF IVADKVTLTS RRAGETTATQ WESAGDGEFT LEEVAKEGRG TEIVLHLKEG
EDEYLSDWSL RSIIRKYSDH ITLPIFMPKT AGYDDEGNIT PAEGVEAVNQ ASALWARPKS
EISDEQYTEF YKHVSHDFEA PLAWSHARVE GKQEYTELLY IPKRAPFDMH DRERRHGIKL
YVRRVFIMED AEKLLPQYLR FVRGLIDSSN LPLNVSREIL QHSKDIEQIK QGCVKKVLGL
LESMANSDDA AEQAKYVTFW EQFGRVMKEG VAEDFANKDR IAGLLRFASS HTDSADQNVS
LAAYVGRMKE GQDKIYFITA DSFAAAKNSP HLEVFRKKGI EVLLMSERVD EWMISGLTEF
DGKKLQSVTK GELDLSNFEN EEEKQQQEAA ASELKDVLDK VKAVLGDKVK DVRVTNRLTD
SPACIVVENQ DMSANLERLL KSAGQDVKGS KPILEINPEH MLVKKLKAEL EGERFGDWTE
LLFDQAQLAE GAQLDDPATF VKRLNSLMIS VAA
//
