ID A0A0C5WNI6_9GAMM Unreviewed; 632 AA.
AC A0A0C5WNI6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-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=H744_2c1228 {ECO:0000313|EMBL:AJR07907.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR07907.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR07907.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR07907.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) 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; CP005974; AJR07907.1; -; Genomic_DNA.
DR RefSeq; WP_044624404.1; NZ_CP005974.1.
DR AlphaFoldDB; A0A0C5WNI6; -.
DR STRING; 658445.H744_2c1228; -.
DR KEGG; pgb:H744_2c1228; -.
DR PATRIC; fig|658445.3.peg.3120; -.
DR HOGENOM; CLU_006684_3_0_6; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000032303; Chromosome 2.
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:UP000032303};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:AJR07907.1}.
FT DOMAIN 33..190
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..344
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 562..632
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 632 AA; 72159 MW; D9411A652E346BE9 CRC64;
MSEQTIHKNK ETRGFQSEVK QLLQLMIHSL YSNKEIFLRE LISNASDAAD KLRFRALSQP
DLYESDAELG VKLSFNEQAG TLTISDNGIG MSRDDVIEHL GTIAKSGTKD FFAKLSEDES
KDSQLIGQFG VGFYSAFIVA DSVTVNTRAA GVAADQAVSW QSSGEGDYTV EDITKETRGT
DIVLHLREEE KEFLSEYRLR DIIGKYSDHI GIPVHIQTVE RDEEGQETGR KWEQINKAQA
LWTRNKSDIS EEEYKEFYKH VSHDFAEPLT WSHNRVEGKQ DYTSLLYIPS KAPWDLYNRE
SKHGLKLYVQ RVFIMDDAEQ FMPSYLRFMR GLIDSNDLPL NVSREILQDN KVTQSLRKAC
TKRALTMMDR LASNDAEKYQ TLWNEFGQVL KEGPVEDFAN REKIAKLLRF SSTHAETVEQ
TVSLADYIER MKEGQDKIYF LTADSFSAAK NSPHLEQFRA KGLEVLLMHD RIDEWLMGHL
PEFEGKQFQA ITKADLDLSA FEQEEEKEKR KETEEAFQSV VERTKTYLGE RVKDVRTTFK
LKETPAVVVT DENEMGTQMA KLLAAAGHDA PEVQYILELN PEHPLVSKMA DEADEEIFGR
WVEMLLGQAM LAEKGTMDDP SQFLAAVNKL LG
//
