ID A0A1B9ASF9_9BACI Unreviewed; 626 AA.
AC A0A1B9ASF9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
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=A8L44_05545 {ECO:0000313|EMBL:OCA86749.1};
OS Bacillus sp. FJAT-27986.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA86749.1, ECO:0000313|Proteomes:UP000092673};
RN [1] {ECO:0000313|EMBL:OCA86749.1, ECO:0000313|Proteomes:UP000092673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA86749.1,
RC ECO:0000313|Proteomes:UP000092673};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J.,
RA Liu B., Liu G.;
RT "Bacillus sp. FJAT-27986.";
RL Submitted (MAY-2016) 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:OCA86749.1}.
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DR EMBL; MAYV01000012; OCA86749.1; -; Genomic_DNA.
DR RefSeq; WP_066103698.1; NZ_MAYV01000012.1.
DR AlphaFoldDB; A0A1B9ASF9; -.
DR STRING; 1743146.A8L44_05545; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000092673; 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 Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00505};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00505}; Reference proteome {ECO:0000313|Proteomes:UP000092673};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 24..177
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..341
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 553..626
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 72709 MW; 2C9E6406BECFCEA5 CRC64;
MEKQQFKAES KRLLEMMINS IYSQREVFLR ELISNASDAI DKLYYKALTD ESLTFNKESY
YIKVSADKEN RTLSILDTGI GMTKEELENN LGTIARSGSL AFKSENESKD GHDIIGQFGV
GFYAAFMVAD KVTVISKALD SDTAYKWESE GTEGYTIVPC EKETIGTEII LTIKENSEEE
DFDQYLDEYK LKSIIKKYSD FIRYPIKMDT VEKHLIEGSE DEYENIIEEQ TINSMVPIWK
KNKSELTDED YESFYHEKHY GFDKPLKHLH INVDGTIRYN AILYIPENIP FDYYSKEFEK
GLELYSNGVL IMEKCADLLP DHFSFVKGMV DSEDLSLNIS REMLQHDRQL KLIAKNISKK
IKSELQSLLK NNREKYDSFY KSFGRQIKFG VYSDFGANKE ALQDLLMFYS SKEKKLVTLD
EYVSRMPEDQ KYIYYATGDS YERIEKLPQT ELVLDEGYEI LYFTEDIDEF AVKMIMNYKE
KEFKSVSSGD LGIDRNSSDK QTDEQEEENT EIFNYMKELL TNKVKDVRAS KRLKTHPVCL
SADGEITIEM EKILNAMPDN QNVKADKVLE INTNHEVFQS LKAAYEQDKS KLDLYTELLY
NQALLIEGLP INDPVEFTNN ICKVMV
//
