ID A0A0R0CDW9_9GAMM Unreviewed; 634 AA.
AC A0A0R0CDW9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=ABB27_16595 {ECO:0000313|EMBL:KRG64295.1};
OS Stenotrophomonas terrae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=405446 {ECO:0000313|EMBL:KRG64295.1, ECO:0000313|Proteomes:UP000051863};
RN [1] {ECO:0000313|EMBL:KRG64295.1, ECO:0000313|Proteomes:UP000051863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18941 {ECO:0000313|EMBL:KRG64295.1,
RC ECO:0000313|Proteomes:UP000051863};
RA Patil P.P., Midha S., Patil P.B.;
RT "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL Submitted (MAY-2015) 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:KRG64295.1}.
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DR EMBL; LDJJ01000064; KRG64295.1; -; Genomic_DNA.
DR RefSeq; WP_057629970.1; NZ_LDJJ01000064.1.
DR AlphaFoldDB; A0A0R0CDW9; -.
DR PATRIC; fig|405446.3.peg.3202; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000051863; 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};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:KRG64295.1}.
FT DOMAIN 30..187
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..342
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 560..634
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 634 AA; 71292 MW; B004E576D20C286B CRC64;
MTDQNHKETR GFQTEVKQLL HLMIHSLYSN KEIFLRELVS NAADAADKLR FEALTQPELL
EGGAPLRIRI EADPVARTLT IDDNGIGLSR DEAIAHLGTI AKSGTAEFLK NLSGDQKKDS
NLIGQFGVGF YSAFIVADQV DVYSRRAGLP ASEGVHWSSR GEGEFEVETI DKPERGTRIV
LHLKEGEDSY TDGWQLRSLI KKYSDHIGLP IELQKEHHGE EADKPATPEW ETVNRANALW
TRPKSEVKDE EYKEFYKHIA HDPTDPLAWT HNKVEGKLEY TSLLYTPGRA PFDLYHRDAP
KGLKLYVQRV FIMDQAEQFL PLYLRFIKGV VDSNDLPLNV SREILQSGPV IDSMKSALTK
RSLDMLEKLA KDKPEDYAGF WKNFGQVLKE GPAEDYGNRE KVAGLLRFAS THDGSGEQSV
ALADYIGRMI EGQDKIYYLT GESFQQVKDS PHLEVFRKKG IEVLLMTDRI DEWLMSYLTE
FDGKSFADIA RGDLDLGKLE SEEDKKAQEE VAKTKEGLAT RLKTALGEEV AEVRVSHRLT
DSPAILAIGE QDLGLQMRQI LEASGQKVPD SKPVFEFNPS HPLIEKLDAE PDMDRFNDLA
HVLFDQAALA AGDSLKDPAG YVRRLNKLLL ELSA
//
