ID A0A1A9EXV1_9GAMM Unreviewed; 641 AA.
AC A0A1A9EXV1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=A8C75_07565 {ECO:0000313|EMBL:ANG62359.1};
OS Marinobacterium aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinobacterium.
OX NCBI_TaxID=1821621 {ECO:0000313|EMBL:ANG62359.1, ECO:0000313|Proteomes:UP000078070};
RN [1] {ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|Proteomes:UP000078070};
RA Baek K., Yang S.-J.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ANG62359.1, ECO:0000313|Proteomes:UP000078070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST58-10 {ECO:0000313|EMBL:ANG62359.1,
RC ECO:0000313|Proteomes:UP000078070};
RX PubMed=29303694; DOI=10.1099/ijsem.0.002561;
RA Bae S.S., Jung J., Chung D., Baek K.;
RT "Marinobacterium aestuarii sp. nov., a benzene-degrading marine bacterium
RT isolated from estuary sediment.";
RL Int. J. Syst. Evol. Microbiol. 68:651-656(2018).
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; CP015839; ANG62359.1; -; Genomic_DNA.
DR RefSeq; WP_067380221.1; NZ_CP015839.1.
DR AlphaFoldDB; A0A1A9EXV1; -.
DR STRING; 1821621.A8C75_07565; -.
DR KEGG; mars:A8C75_07565; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000078070; 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}; Reference proteome {ECO:0000313|Proteomes:UP000078070};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505}.
FT DOMAIN 30..187
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..349
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 567..641
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 641 AA; 71943 MW; 0803CAE478C93B83 CRC64;
MSTETQKETL GFQTEVKQLL HLMIHSLYSN KEIFLRELIS NASDAAEKLR FEALSNADLY
ENDGDIRIRV SFDEAAKTIT IDDNGIGMSR QDVIDHLGTI AKSGTSGFLS QLTGDQKKDS
QLIGQFGVGF YSAFIVADKV DVFSRRAGLA AAEGVHWSSR GEGEFSIATL EKESRGTSIV
LHLKEEEAEF ANSWRLRELV RKYSDHIALP VVMQKDAVEP EEPEEGQEPT PVAAPQDETV
NSATALWTRS KSEVTDEEYS EFYKHVSHDF NDPLSWSHSK VEGSLEYSSL LYVPEKAPYD
LWNREAPRGL KLYIQRVFIM DQADQFLPLY LRFIKGVVDS SNLSLNISRE ILQKDPHVDK
LRAALSKRAL DMLAKLAKND ADKYQAFWKE FGQVLKEGPA EDHANREKVL KLLRFASTHT
GTSDQNVGLD DYVARMQEGQ SKIYYVVADS FNAAKSSPHL EIFRKKGIEV LLLTDRIDEW
MMSHLFDFDG KSFQDVSKGE LDLGEVENEE EKAAQEATAK ELSGLVERLK TQLGERVSDV
RITHRLTDSP ACVVLGSYDM GAQMRRIMEA AGQPVPEVKP VFELNPAHPL IQKLDQEVDE
DRFGELSLVI FDQAGLAAGG QLDDPAAYVA RLNKLLLELS Q
//
