ID I0HBB3_ACTM4 Unreviewed; 619 AA.
AC I0HBB3;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 OrderedLocusNames=AMIS_50800 {ECO:0000313|EMBL:BAL90300.1};
OS Actinoplanes missouriensis (strain ATCC 14538 / DSM 43046 / CBS 188.64 /
OS JCM 3121 / NBRC 102363 / NCIMB 12654 / NRRL B-3342 / UNCC 431).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=512565 {ECO:0000313|EMBL:BAL90300.1, ECO:0000313|Proteomes:UP000007882};
RN [1] {ECO:0000313|EMBL:BAL90300.1, ECO:0000313|Proteomes:UP000007882}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14538 / DSM 43046 / CBS 188.64 / JCM 3121 / NBRC 102363 /
RC NCIMB 12654 / NRRL B-3342 / UNCC 431
RC {ECO:0000313|Proteomes:UP000007882};
RA Ohnishi Y., Ishikawa J., Sekine M., Hosoyama A., Harada T., Narita H.,
RA Hata T., Konno Y., Tutikane K., Fujita N., Horinouchi S., Hayakawa M.;
RT "Complete genome sequence of Actinoplanes missouriensis 431 (= NBRC
RT 102363).";
RL Submitted (FEB-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012319; BAL90300.1; -; Genomic_DNA.
DR AlphaFoldDB; I0HBB3; -.
DR STRING; 512565.AMIS_50800; -.
DR KEGG; ams:AMIS_50800; -.
DR PATRIC; fig|512565.3.peg.5075; -.
DR eggNOG; COG0326; Bacteria.
DR HOGENOM; CLU_006684_3_0_11; -.
DR Proteomes; UP000007882; 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:UP000007882};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00505,
KW ECO:0000313|EMBL:BAL90300.1}.
FT DOMAIN 26..180
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
FT REGION 1..331
FT /note="A; substrate-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
FT REGION 542..619
FT /note="C"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00505"
SQ SEQUENCE 619 AA; 69758 MW; 1A6FEDEA0487C005 CRC64;
MTMETLEFQA EARQLLQLMV HSIYSNKDIF LRELISNASD ALDKLRLAKL QDGLEADTSD
LHIEIEADPE SRTLTVRDNG IGMTREEVVE LIGTIAKSGT AELLTKLKEA KESPELIGQF
GVGFYSTFMV ADKVTLVTRK AGTDGHGTRW ESAGEGTYSI DDAPDTPVGT TVTLHLRPKD
EEDALYDYAE EWKIKEIVKK YSDFISFPIR YVSAAGEEGE TLNSMKALWA RPRSEVTDEE
YHQFYRHISH DWTDPLEIIN MKAEGTFEYE ALLFIPARAP FDLFQRDARR GLQLYVKRVF
IMDDSKELIP DYLRFVKGVV DAADLSLNIS REILQQDRHI QMIRRRLTKK VLSTIKEMMT
GSPEKYATFW REFGRAIKEG LLSEPDNHKP ILEIASFGTT HGEEPTTLAA YVERMKEGQE
EIYFLTGESR SQVENSPHME AFREQGYEVL VLTDPVDEIW VDAVTEFDGR KLRSIARGSV
DLKKDASEGD EAAEGDFAPL LTFLKEKLDD QVKEVRLSHR LTTSAACLVS DADDITPALE
KMYRAMGQEG PRVKRILELN PGHPLVSGLR AAFERGADDA TLPDTAELLY GTALLAEGGD
LEDPARFAKL LADRLARTV
//
