ID K1ZEI8_9BACT Unreviewed; 589 AA.
AC K1ZEI8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EKD36364.1};
DE Flags: Fragment;
GN ORFNames=ACD_75C01535G0001 {ECO:0000313|EMBL:EKD36364.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD36364.1};
RN [1] {ECO:0000313|EMBL:EKD36364.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23019650; DOI=10.1126/science.1224041;
RA Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA Long P.E., Banfield J.F.;
RT "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT bacterial phyla.";
RL Science 337:1661-1665(2012).
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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:EKD36364.1}.
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; AMFJ01032204; EKD36364.1; -; Genomic_DNA.
DR AlphaFoldDB; K1ZEI8; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:InterPro.
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; IPR036890; HATPase_C_sf.
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:SF44; HEAT SHOCK PROTEIN 75 KDA, MITOCHONDRIAL; 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 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.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKD36364.1"
SQ SEQUENCE 589 AA; 66155 MW; B827B05AC8A078C0 CRC64;
SNAADALEKL RHESITKTDI FDGHLPLEIT IDLDEKNNTL TIIDTGIGMS RSEMEHNLGT
IAHSGSNTFM AELVEAAKKD VSLIGQFGVG FYSAFMAGKI VRVQSRSWDK SEGHEWVSDG
TGSFTITEMP GLRRGTKVIV ELKEEAKEYV QKWKISSVVK QYSAFVSFPI KLDGETINTI
QALWTRNKSD IKEEEYVEFY KFIGNAGTEP LYRLHFSADA PLAINALLFV PAENFEVFGF
GKVDPGVNLY CQRILIDQHS KNILPDWLRF LKGVVDSEDL PLNISRQALQ DNALVAKIRK
VITKRFLKYL DEEAKSDPEK YLKFWTTFGI YIKEGVTSDY EFQKELGKLL RFESSKSAEG
KPVALADYLL RMAPDQQEIY YINGPSRAAV EAGPYVEMFR KKDIEIIYTM EPIDDFVLSH
LAEFEGKKLV SADRADLAVK EEDEAKEDGG EGAESGKLDK DALATLTDWM KKVLETHVSE
VVVSKRLVDA PAMIVNPDAF MTSTMERVLA AGRKEKGIPG MGVTKKKLEI NPRNPLIKKL
AELFQRDEDF AAEIARQIHD NAMIQAGLVV DPLAMVERNY RILNRVVGG
//
