ID A0A163WNU2_9FLAO Unreviewed; 618 AA.
AC A0A163WNU2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:KZE76607.1};
GN ORFNames=AV926_15815 {ECO:0000313|EMBL:KZE76607.1};
OS Myroides marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=703342 {ECO:0000313|EMBL:KZE76607.1, ECO:0000313|Proteomes:UP000076630};
RN [1] {ECO:0000313|EMBL:KZE76607.1, ECO:0000313|Proteomes:UP000076630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L41 {ECO:0000313|EMBL:KZE76607.1,
RC ECO:0000313|Proteomes:UP000076630};
RA Hong K.W.;
RT "Whole genome sequencing of Myroides marinus L41.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:KZE76607.1}.
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DR EMBL; LQNU01000076; KZE76607.1; -; Genomic_DNA.
DR RefSeq; WP_038986020.1; NZ_LQNU01000076.1.
DR AlphaFoldDB; A0A163WNU2; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000076630; Unassembled WGS sequence.
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 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 SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 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};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
SQ SEQUENCE 618 AA; 70629 MW; 40F022E9C01284FC CRC64;
MTSGKINVTV ENIFPLIKKF LYSDHEIFLR ELISNATDAT LKLKHLTTIG ETNVEYGDPI
IEVKIDKENK KLHIIDQGLG MTKDEVEKYI NQVAFSGAEE FLEKYKDSAK DTGIIGHFGL
GFYSAFMVAD KVEIFTKSFK DEPAAHWTCD GSPEYTLEAC DKTDRGTEIV LHIAEDSLDF
LEDYKIRELL VKYNKFMPVA IKFGTHEEGE GDDKVLVDTI INNPSPAWTK QPADLNDEDY
KNFYRELYPT QFEEPLFHIH LNVDYPFNLT GILYFPKLSA DLQMQKDKIQ LYQNQVFVTD
NVEGIVPDFL TMLKGVIDSP DIPLNVSRSY LQADGNVKKI SNYITRKVAD KLKSLFNENR
EDFESKWNDI KIVLEYGMLS EEKFYEKANS FVLYPTVEDK FYTLEELKEA TKDNQTDKDD
NLVILYASNK DAQHSYIAAA KDKGYQVVLL DSPIVSHLIQ KLESDNEKMT FVRVDADHIN
NLIKKDETEI SRLSEDEQKS LQDIVENIVP KDKYTVKLEA MDSTAEPFII TQPEFMRRMK
EMSQSGGGGM FGMGNFPEMY NLVVNTNSPL ASNIISNTDE ATRTESIKQA MDLAKLSQGL
LKGEELTAFV KRNFNNLK
//
