ID A0A1M6W7F4_9BACT Unreviewed; 613 AA.
AC A0A1M6W7F4;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Molecular chaperone HtpG {ECO:0000313|EMBL:SHK89549.1};
GN ORFNames=SAMN05444266_101512 {ECO:0000313|EMBL:SHK89549.1};
OS Chitinophaga jiangningensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=1419482 {ECO:0000313|EMBL:SHK89549.1, ECO:0000313|Proteomes:UP000184420};
RN [1] {ECO:0000313|EMBL:SHK89549.1, ECO:0000313|Proteomes:UP000184420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27406 {ECO:0000313|EMBL:SHK89549.1,
RC ECO:0000313|Proteomes:UP000184420};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000256|ARBA:ARBA00008239}.
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DR EMBL; FRBL01000001; SHK89549.1; -; Genomic_DNA.
DR RefSeq; WP_073077702.1; NZ_FRBL01000001.1.
DR AlphaFoldDB; A0A1M6W7F4; -.
DR STRING; 1419482.SAMN05444266_101512; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000184420; 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; IPR003594; HATPase_C.
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: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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000184420}.
FT DOMAIN 24..178
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 613 AA; 70218 MW; F0C339B0566700C2 CRC64;
MQKGAIRVQT ENIFPIIKKF LYSDHEIFIR ELVSNAVDAT QKLRTLASVG EFKGDLGNID
IEVKLDKEKK TITIADHGVG MTAEEVDKYI NQVAFSGAEE FLKKYKGQES GTNIIGHFGL
GFYSSFMISN QVEIFSKSWK EDAPAVRWEC DGSPEYSLEE TTKTERGTEI VMHVNEESEE
FLDEGRIRSI LTKFCKFLPV PVKFEGEQIN NVAPAWTKKP SELTAEDYQN FYKELYPFAE
APLFWIHLNV DYPFNLTGIL YFPKITKSYE IQKDKINLYS NQVYVTDEVK DIVPEFLMLL
HGVIDSPDIP LNVSRSYLQG DPNVKKINGY ITKKVADKLD EMFRQDRKSF EEKWESIGLF
VKYGMMTDDK FLDKANKFLL LEDVADGKFY TQEEYRTETA ALQTNKEGKL VVLYSTNPVQ
QDSYIQAAQK KGFKVVKMET LVDAAFINNI EMKWDNVQFT RVDADIANNL IDKDENADTL
LSKEQEETLK NLFTQEVNQP NIKVDMKGLT ADLQPVIVTR PEFMRRMKDM ASMGGGGMNW
YANMPDEINM TINANHPVYL QILREKNNGL QQKQIKNLAD LALLSQNLLT GADLTAFVNR
SVELMSKEEE EEA
//
