ID R5INP4_9CLOT Unreviewed; 669 AA.
AC R5INP4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Molecular chaperone HtpG {ECO:0008006|Google:ProtNLM};
GN ORFNames=BN757_02835 {ECO:0000313|EMBL:CCY43710.1};
OS Clostridium sp. CAG:7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262832 {ECO:0000313|EMBL:CCY43710.1, ECO:0000313|Proteomes:UP000018268};
RN [1] {ECO:0000313|EMBL:CCY43710.1, ECO:0000313|Proteomes:UP000018268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:7 {ECO:0000313|Proteomes:UP000018268};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCY43710.1}.
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DR EMBL; CAYE010000139; CCY43710.1; -; Genomic_DNA.
DR AlphaFoldDB; R5INP4; -.
DR STRING; 1262832.BN757_02835; -.
DR Proteomes; UP000018268; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000018268}.
SQ SEQUENCE 669 AA; 77515 MW; F4E63970F13ACEE4 CRC64;
MAKKGSLSIT SENIFPVIKK WLYSDHDIFY RELISNGCDA ITKLKKLELM GEYEKPEEVE
YKIQVSVNPT DKTITIEDNG LGMTEEEIDK YINQIAFSGV QDFMEKYKDK ANEDQIIGHF
GLGFYSAFMV ADKVEINSLS YQKDAKPVHW ESEGGINFEM AEGDKKEVGT SIKLYLNEES
TEFANEYRAR EVIEKYCAFM PVNIFLKNET AEPEYETIEK DELTHKDTVV ETVIEPAKTE
EKEKEDGTKE TVEVEPSREK YKILKRPVAL NDTDPLWNKH PNECTDEQYK DFYRKVFRDY
KEPLFWIHLN MDYPFNLKGI LYFPKINMEY DSLEGTIKLY NNQVFIADNI KEVIPEFLML
LKGVIDCPDL PLNVSRSALQ NDGFVKKISD YITKKVADKL SGMCKTDREN YEKYWDDIAP
FIKFGYIKDE KFAEKMGDYI LYKNLEGKYL TLNDCLEENK EKHENTIFYV TNEKEQSQYI
NLFKEEGIDA VIMPAAIDNP FISHVEQKHE GLKFLRIDTD LNASFKEEVK EDDEAFKKTS
EELTEVFKKA LNNDKLDIKV EKMKNASVAS MITVSEETRR MQDMMKMYSM GGMDMSAFGA
TGETLVLNAN HPLVKYVLEN KEGENTVKIC EQLYDLASLA HGQLSPERMT NFVNRSNDIM
MIMAGQKAE
//