ID X2H6Q2_9NEIS Unreviewed; 632 AA.
AC X2H6Q2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=SALWKB2_0713 {ECO:0000313|EMBL:AHN28095.1};
OS Snodgrassella alvi wkB2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Snodgrassella.
OX NCBI_TaxID=1196094 {ECO:0000313|EMBL:AHN28095.1, ECO:0000313|Proteomes:UP000019668};
RN [1] {ECO:0000313|EMBL:AHN28095.1, ECO:0000313|Proteomes:UP000019668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WkB2 {ECO:0000313|EMBL:AHN28095.1};
RX PubMed=25053814;
RA Kwong W.K., Engel P., Koch H., Moran N.A.;
RT "Genomics and host specialization of honey bee and bumble bee gut
RT symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:11509-11514(2014).
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; CP007446; AHN28095.1; -; Genomic_DNA.
DR RefSeq; WP_025330326.1; NZ_CP091515.1.
DR AlphaFoldDB; X2H6Q2; -.
DR STRING; 1196094.SALWKB2_0713; -.
DR GeneID; 32537427; -.
DR KEGG; salv:SALWKB2_0713; -.
DR PATRIC; fig|1196094.4.peg.713; -.
DR HOGENOM; CLU_006684_3_0_4; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000019668; 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; 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|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00505}.
FT DOMAIN 25..182
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..338
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 556..632
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 632 AA; 70927 MW; 619C964C1A402D16 CRC64;
MKQTHSFQTE VKQLLQLMIH SLYSNKEIFL RELISNAADA CDKLRFESLN DASLLGDDTE
FRIKVTADAE AKTITVSDNG IGMTEADIIE HLGTIAKSGT KAFLEKLTGD DKKDANLIGQ
FGVGFYSAFI VADKVTVESR RAGAAENQAV RWVSAGDGEF TVEPISKSAR GTDVILHLKD
DEKDLLSDWT LRRIVTTYSD HISVPIYMKK APEYDEEGNV KVSDELEVVN QAQALWQRPK
NEITDEQYQT FYRHVSHDYD DALAWTHFRV EGRHEYTGLL YIPKHAPFDL YEREPKHGVQ
LYVKRVFIMD DAKKLMPSYL RFIRGVIDSS DLPLNVSREI LQESRDLDAI RSGSVKKVLS
LLEDLKKNQP EKYAEFWQVF GNTLKEGIAE DFTNKDKIAG LCRFASTHND SSEQNVTLAD
YIGRMKEGQE KIYYITADSY AAAKNSPHLE IFLKKGVEVL LLTDRVDEWV VNSLSEFDGK
GLVSVAKGSL DLGNLADEEE KAAQAKTEED NKELVEQIKT ALGDKVDAVR ATARLTESPA
CLVVGEHDMS QHLARMLEAS GAAGQIPQTK PTLEINPDHP LIKKIASEQD EVQRNELAEL
VYDQALLAEG GKLENPAAFV KRMNHLLLTL NQ
//
