ID L8JIP8_9GAMM Unreviewed; 633 AA.
AC L8JIP8;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, 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=C942_01240 {ECO:0000313|EMBL:ELR67312.1};
OS Photobacterium marinum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=1056511 {ECO:0000313|EMBL:ELR67312.1, ECO:0000313|Proteomes:UP000011134};
RN [1] {ECO:0000313|EMBL:ELR67312.1, ECO:0000313|Proteomes:UP000011134}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK15 {ECO:0000313|EMBL:ELR67312.1,
RC ECO:0000313|Proteomes:UP000011134};
RA Khatri I., Vaidya B., Srinivas T.N.R., Subramanian S., Pinnaka A.;
RT "Genome Assembly of Photobacterium sp. AK15.";
RL Submitted (DEC-2012) 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:ELR67312.1}.
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DR EMBL; AMZO01000002; ELR67312.1; -; Genomic_DNA.
DR RefSeq; WP_007461688.1; NZ_AMZO01000002.1.
DR AlphaFoldDB; L8JIP8; -.
DR PATRIC; fig|1056511.3.peg.312; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000011134; 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 33..190
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..345
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 563..633
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 633 AA; 72229 MW; 09034B6BF2830001 CRC64;
MSEQTTHKNK ETRGFQSEVK QLLHLMIHSL YSNKEIFLRE LISNASDAAD KLRFRALSQS
DLYENDAELG VKLSYNEEAG TLTVSDNGIG MTRDEVIEHL GTIAKSGTKD FFAKLSEEET
KDSQLIGQFG VGFYSAFIVA DAVTVNTRAA GTPADQAVRW HSTGEGDYSV EDIEKAGRGT
EIILHLREEE KEFLSEYRLR DIIGKYSDHI GIPVQIQTAE RDEEGKETGN KKWEQINKAQ
ALWTRNKSDI TDEEYQEFYK HVSHDFAEPL IWSHNRVEGK QDYTSLLYIP SKAPWDMYNR
DSKHGLKLYV QRVFIMDDAQ QFMPSYLRFM RGLIDSNDLP LNVSREILQD NKVTQSLRKA
CTKRALTMME RLANNDAEKY QTLWDEFGQV LKEGPAEDFA NRDKIAKLLR FSSTHTDSTE
QNVSLAAYVE RMKEGQDKIY YLTADTFTAA KNSPHLEQFR AKGLEVLLMH DRIDEWLMGN
LPEFDGKAFQ AITKADLDLS TFEDEEEKEK HKETEEAFQS VIERTKSYLG ERVQDVRATF
KLHDTPAVVV TGEHEMGTQM AKLLAAAGHE APEVKYILEL NPEHKLVNKM ADEADEEQFG
LWVEMLLGQA LLAERGSVED PSQFLSAVNK LLA
//
