ID A0A1E5INP2_SHECO Unreviewed; 639 AA.
AC A0A1E5INP2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=BEL05_03945 {ECO:0000313|EMBL:OEG72152.1};
OS Shewanella colwelliana (Alteromonas colwelliana).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=23 {ECO:0000313|EMBL:OEG72152.1, ECO:0000313|Proteomes:UP000095230};
RN [1] {ECO:0000313|EMBL:OEG72152.1, ECO:0000313|Proteomes:UP000095230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSB03KR {ECO:0000313|EMBL:OEG72152.1,
RC ECO:0000313|Proteomes:UP000095230};
RA Hong H.-H., Choi H., Cheon S., Oh J.-S., Lee H.-G., Park C.;
RT "Whole-genome of two Shewanella species isolated from a digestive organ of
RT sea cucumber Apostichopus japonicus Selenka 1867.";
RL Submitted (JUL-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:OEG72152.1}.
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DR EMBL; MCBT01000048; OEG72152.1; -; Genomic_DNA.
DR RefSeq; WP_069672063.1; NZ_MCBT01000048.1.
DR AlphaFoldDB; A0A1E5INP2; -.
DR STRING; 23.BEL05_03945; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000095230; 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}; Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 27..184
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..347
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 565..639
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 639 AA; 71754 MW; 3D6EB8405E440083 CRC64;
MSQQETHGFQ TEVKQLLNLM IHSLYSNKEI FLRELVSNAA DAADKLRYEA LTNDALYEGD
GELRVRISAD KEKGTVTIED NGIGMTRDSV IEHLGTIAKS GTADFFKNLS GDESKDSQLI
GQFGVGFYSA FIVADKVTVR TRAAGHAHDE AVQWESAGEG DFTVETITKE TRGTEITLHL
REEEKEFADD YRLRSIITKY SDHISVPVEM WQEGTPAQEA TEEGAEAIPA TEGEWKGMNK
ATALWTRSKS DVSDEEYQEF YKHISHDFVD PLLWSHNRVE GKQEYTSLLY IPAKAPWDLW
NRDRKHGLKL FVQRVFVMDD AEQFMPSYLR FVQGLIDSND LPLNVSREIL QDNKVTTALR
TAVTKRVLGM LEKLAKNDAE KYQTFWTEFG QVLKEGPAED FANKEKIAGL LRFASTHTNE
AAHTVSLADY ISRMKEGQNK IYYIVADSHE AAANSPHLEL LRKKDIEVLL MSERIDEWLI
NHLTEFDGKQ LHSVTRGDLE LGDLEDAGEK EAQEKLETES EGLVTRVKDA LGDRVSAVKV
TTRLTDTPAC VVAGEGEMSS QMIKLMQAAG QAVPESKPVF ELNPEHPLVA RLDGEQDEEL
FSQWADLLLQ QAQLSEKGSL ADPSAFIKLM NKMLLAGAK
//
