ID A0A1M6C3L8_9FIRM Unreviewed; 666 AA.
AC A0A1M6C3L8;
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:SHI55364.1};
GN ORFNames=SAMN02745691_00458 {ECO:0000313|EMBL:SHI55364.1};
OS Parasporobacterium paucivorans DSM 15970.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Parasporobacterium.
OX NCBI_TaxID=1122934 {ECO:0000313|EMBL:SHI55364.1, ECO:0000313|Proteomes:UP000184342};
RN [1] {ECO:0000313|EMBL:SHI55364.1, ECO:0000313|Proteomes:UP000184342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15970 {ECO:0000313|EMBL:SHI55364.1,
RC ECO:0000313|Proteomes:UP000184342};
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; FQYT01000004; SHI55364.1; -; Genomic_DNA.
DR RefSeq; WP_073992750.1; NZ_FQYT01000004.1.
DR AlphaFoldDB; A0A1M6C3L8; -.
DR STRING; 1122934.SAMN02745691_00458; -.
DR OrthoDB; 9802640at2; -.
DR Proteomes; UP000184342; 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; 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000184342}.
FT COILED 523..555
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 666 AA; 76709 MW; 940BFF7B7ABC520A CRC64;
MAGKQGSLSI NSENIFPIIK KWLYSDHDIF IRELISNGSD AITKLKKLDV IGEYSIPEGN
EFKIRVIADA ENKTLTFIDN GIGMTAGEVD EYINQIAFSG AEAFLEHYKG KADEEQIIGH
FGLGFYSAFM VSEKVTIDSL SYREGAEAVH WDCDGSTEYT MDKGDRTERG TTITLYLNED
SLEFANEYRV HEVLDKYCSF MPVEIYLENP NAEPHYDTVD PDEVTEKDTV IENIVIPAET
QEIEKEDGAK ETIQVSPEKN QVKILRRPVS ISDTAPLWTK HPNECTEEEY IAFYRKVFSD
YKKPLFWIHL NMDYPFNLKG ILYFPKVNNQ YESLEGTIKL FNNQVFIADN IKEVIPEFLM
LLKGVIDCPD LPLNVSRSAL QNDGFVRKIS DYISKKVADK LTGMCKTEKD EYIKYWDDIS
PFIKFGCLKD EKFAEKINDC ILFKNLDNEY LTLKECLEKN EEKHKNVIFY ITDEVAQSQY
INMFREENID AVRLTHSIDS AFITQLEHKN EDVKFLRIDT ALNESLREEI PDADKEAAEA
EEASLTELFR KALENENLNI KMEYLKNKNI SSMITVSEES HRMQEMFKMY AMDGIDAGMF
GAEETLVLNA NNQLVRYILA NRDSEHVDLI CRQLYDLAAI SKKQLTPEAM TEFIARSNEI
MMLLTK
//
