ID A0A145WNM1_9GAMM Unreviewed; 639 AA.
AC A0A145WNM1;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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=AMD27_01285 {ECO:0000313|EMBL:AMW77663.1};
OS Acinetobacter sp. TGL-Y2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1407071 {ECO:0000313|EMBL:AMW77663.1, ECO:0000313|Proteomes:UP000076238};
RN [1] {ECO:0000313|Proteomes:UP000076238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TGL-Y2 {ECO:0000313|Proteomes:UP000076238};
RA Zhang G.;
RL Submitted (APR-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}.
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DR EMBL; CP015110; AMW77663.1; -; Genomic_DNA.
DR RefSeq; WP_067655281.1; NZ_CP015110.1.
DR AlphaFoldDB; A0A145WNM1; -.
DR STRING; 1407071.AMD27_01285; -.
DR KEGG; acv:AMD27_01285; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000076238; Chromosome.
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; 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.
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|ARBA:ARBA00022490, 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:UP000076238};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 29..186
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..351
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 571..639
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 639 AA; 71635 MW; 858CE4F092691B5E CRC64;
MSEQNTQKHS FQAEVAQLLH LVTHSLYSNP EIFLRELISN ASDACDKLRF EGINHPEFYE
NDPDLHVRVT LDKDNKTITI SDNGIGLSQQ EAIDNLGTIA KSGTKDFMSK LSGDQKSDAQ
LIGQFGVGFY SGFIVAEKIT VESRRAGTEA TEGVRWISTG TGDFEVAQIE KASRGTDIIL
HLRDDALEYL ETQKVKQIIN KYSDHISLPI EMQKEIWQQE EAVEGEETKP GHYVKTDEWE
AINSASALWT RSKSEITEEQ YVEFYKNLSH DYEAPLAWAH NRVEGSTEYT QLLYIPSKAP
HNIFTREAKA GIKLYVKRVF IMDDADNLIP NYLRFVQGVV DSADLPLNVS RELLQESRDV
KTIREGNARR VLTTLDALAK SEDEADQEKF KTFYTEFGSV IKEGLGEDLG NRDRILKLLR
FATSTSDEVN TTFAAYKEVM KEGQKAIYYV TADSLAAAKN SPQLELFKKK GIQVLLMTDR
VDEWAMEFVH EFDGTPLQNV SKGAVDLGDL QDAEEKKALE AAAEQFKPVV DQLSDALKAK
TSEVRVTTRL VDSPACLVTS EGELSPQLIR MLKQAGQEVP ESKPILEINP EHPLVKKLEG
SAQFDDLANV IFDQAVIAEG GLPSDPAEYL KRINSLLLK
//
