ID A0A0J5P4H5_9PAST Unreviewed; 626 AA.
AC A0A0J5P4H5;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=RO21_06830 {ECO:0000313|EMBL:KMK51328.1};
OS Muribacter muris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Muribacter.
OX NCBI_TaxID=67855 {ECO:0000313|EMBL:KMK51328.1, ECO:0000313|Proteomes:UP000036270};
RN [1] {ECO:0000313|EMBL:KMK51328.1, ECO:0000313|Proteomes:UP000036270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ackerman80-443D {ECO:0000313|EMBL:KMK51328.1,
RC ECO:0000313|Proteomes:UP000036270};
RA Christensen H., Nicklas W., Bisgaard M.;
RT "Reclassification of Actinobacillus muris as Muribacter muris.";
RL Submitted (DEC-2014) 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:KMK51328.1}.
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DR EMBL; JWIZ01000038; KMK51328.1; -; Genomic_DNA.
DR RefSeq; WP_047977054.1; NZ_JWIZ01000038.1.
DR AlphaFoldDB; A0A0J5P4H5; -.
DR STRING; 67855.RO21_06830; -.
DR PATRIC; fig|67855.3.peg.1373; -.
DR Proteomes; UP000036270; 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:UP000036270};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:KMK51328.1}.
FT DOMAIN 28..183
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 555..626
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 71052 MW; 27BCEC926ADC9820 CRC64;
MSTNQETRGF QSEVKQLLQL MIHSLYSNKE IFLRELISNA SDAADKLRFK ALSQPELYEG
DGELRVRISV DETLGTLTIS DNGIGMNREQ VIDHLGTIAK SGTKEFLNAL GADQAKDSQL
IGQFGVGFYS SFIVADKVTV KTRAAGESQG VLWESAGEGD YTVADIEKSG RGTDVILHLR
EEEKEFLSEW RLREIIGKYS DHIGLPVEIQ TKEYDDEGKE TGTKWEKINK AQALWTRAKN
EISDDEYKEF YKHLSHDFAD PLLWSHNKVE GKQEYTSLLY VPSKGPWDLF NRDHKHGLKL
YVQRVFIMDD AELFMPNYLR FMRGLLDSND LPLNVSREIL QDNKTTAALR SALTKRALQM
LEKLAKDDAE KYQTFWKEFG LVLKEGVGED FANKAQVAGL LRFASTHSDS NEQAVSLSDY
LARMKEGQKA IYFLTADSYT AAKNSPHLEL FNKKGIEVLL LSDRIDEWMI GHLTEFDGKP
LQSITKSDLD LGELADKQEE EAQKAQEAEF GSFLERTQNY LGERVKKVAL THRLTDTPAI
VSTDNDEMTT QMAKLFAAMG QTAPEVKYTF ELNPEHAMIK RIADIADESE FNDWIELLFD
QALLAERGTL ENPTAFIKRM NRLLSV
//
