HTPG_METC4
ID HTPG_METC4 Reviewed; 626 AA.
AC B7KPG0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Chaperone protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=Heat shock protein HtpG {ECO:0000255|HAMAP-Rule:MF_00505};
DE AltName: Full=High temperature protein G {ECO:0000255|HAMAP-Rule:MF_00505};
GN Name=htpG {ECO:0000255|HAMAP-Rule:MF_00505}; OrderedLocusNames=Mchl_1155;
OS Methylorubrum extorquens (strain CM4 / NCIMB 13688) (Methylobacterium
OS extorquens).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=440085;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CM4 / NCIMB 13688;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Marx C., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium chloromethanicum
RT CM4.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Molecular chaperone. Has ATPase activity. {ECO:0000255|HAMAP-
CC Rule:MF_00505}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00505}.
CC -!- SIMILARITY: Belongs to the heat shock protein 90 family.
CC {ECO:0000255|HAMAP-Rule:MF_00505}.
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DR EMBL; CP001298; ACK82043.1; -; Genomic_DNA.
DR RefSeq; WP_012606035.1; NC_011757.1.
DR AlphaFoldDB; B7KPG0; -.
DR SMR; B7KPG0; -.
DR EnsemblBacteria; ACK82043; ACK82043; Mchl_1155.
DR KEGG; mch:Mchl_1155; -.
DR HOGENOM; CLU_006684_3_0_5; -.
DR OMA; MRRMKEM; -.
DR BioCyc; MEXT440085:MCHL_RS05535-MON; -.
DR Proteomes; UP000002385; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR Gene3D; 1.20.120.790; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR HAMAP; MF_00505; HSP90; 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_S5_D2-typ_fold.
DR PANTHER; PTHR11528; PTHR11528; 1.
DR Pfam; PF00183; HSP90; 1.
DR PIRSF; PIRSF002583; Hsp90; 1.
DR PRINTS; PR00775; HEATSHOCK90.
DR SUPFAM; SSF110942; SSF110942; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR PROSITE; PS00298; HSP90; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Stress response.
FT CHAIN 1..626
FT /note="Chaperone protein HtpG"
FT /id="PRO_1000146007"
FT REGION 1..331
FT /note="A; substrate-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 332..544
FT /note="B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT REGION 545..626
FT /note="C"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ SEQUENCE 626 AA; 69409 MW; 843EA020B5EDCCB8 CRC64;
MSETVERHEF GAEVGRLLDL VVHALYSDRE IFLRELVANA ADATDRRRFE ALTNEALALP
SDARVLIAPD KAARTLTISD AGIGMSKEDL AQNLGTIARS GTRAFSQALG ERAAEGGEDQ
RPSLIGQFGV GFYSAFMVAD RVTVTSRRAG SEEAWTWASD GKGSYTLEPA SREQPGTDIV
LHMKEDADEY LESYRLDHVV RKWADNIAVP IAIRDAEGKE EAANRGTALW RKPKSEITEE
QYKEFYRTVS HGFDEPWATL HWRAEGALEF TGLLFVPSMK PFMPMEDDRR SKVRLHVRRM
FITDEAELLP NWLRFVHGVV DTDDLPLNVS REMLQSTPTL QKIRRAVTTR VINELSSRSK
NTEKAEEYQK FFENFGPVLK EGIYEDFERR AEIAPLLRFR SSTEGGWTSL PEYVARMKPE
QEAIYYLVAD DVEALKNSAQ LEGFRARRVE VLLLSDHVDA FWPEQLGKFE DKPLRSVTQG
SADLAKLKPE GETAEAAPAL DTLVAALKLA LEPDVSDVRT TDRLVDSAVV LATSGMGPDL
QMQRLLRRAG RGFGGSAPIL EINPRHALIR SLNERAEAGE DLKAEAGTLL DLARVQDGDT
PRDPVAFARA VAAALAGTAA KPAGSA