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HTPG_RHIME
ID   HTPG_RHIME              Reviewed;         629 AA.
AC   P58477;
DT   13-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 118.
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=RB0849;
GN   ORFNames=SMb21183;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OG   Plasmid pSymB (megaplasmid 2).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481431; DOI=10.1073/pnas.161294698;
RA   Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA   Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT   "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT   endosymbiont Sinorhizobium meliloti.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
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; AL591985; CAC49249.1; -; Genomic_DNA.
DR   PIR; A95948; A95948.
DR   RefSeq; NP_437389.1; NC_003078.1.
DR   RefSeq; WP_010975705.1; NC_003078.1.
DR   AlphaFoldDB; P58477; -.
DR   SMR; P58477; -.
DR   STRING; 266834.SM_b21183; -.
DR   EnsemblBacteria; CAC49249; CAC49249; SM_b21183.
DR   GeneID; 61600824; -.
DR   KEGG; sme:SM_b21183; -.
DR   PATRIC; fig|266834.11.peg.5780; -.
DR   eggNOG; COG0326; Bacteria.
DR   HOGENOM; CLU_006684_3_0_5; -.
DR   OMA; MRRMKEM; -.
DR   Proteomes; UP000001976; Plasmid pSymB.
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; 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_S5_D2-typ_fold.
DR   PANTHER; PTHR11528; PTHR11528; 1.
DR   Pfam; PF00183; HSP90; 1.
DR   PIRSF; PIRSF002583; Hsp90; 1.
DR   PRINTS; PR00775; HEATSHOCK90.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF110942; SSF110942; 1.
DR   SUPFAM; SSF54211; SSF54211; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Cytoplasm; Nucleotide-binding; Plasmid;
KW   Reference proteome; Stress response.
FT   CHAIN           1..629
FT                   /note="Chaperone protein HtpG"
FT                   /id="PRO_0000063008"
FT   REGION          1..335
FT                   /note="A; substrate-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          336..551
FT                   /note="B"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
FT   REGION          552..629
FT                   /note="C"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00505"
SQ   SEQUENCE   629 AA;  69295 MW;  85C872C63654D801 CRC64;
     MSEVETSVEK HVFEADVAKL LHLMVHSVYS DKNVFLRELI SNAADACEKL RYEAIVAPEL
     LGSDPASRIT LTLDEENARL VIEDNGIGMG RDELVESLGT IARSGTRAFM ERIEAAQNKD
     GAQLIGQFGV GFYSAFMVAD NVDVVSRRAG TDKAWHWASD GKGSYTVSAV DLADAPARGT
     RITLHLMDEA KTFTSRWTVE RIVKEQSGHV PVPISIVEKP GAEPAQVADG TALWTKQKSE
     ISKDDYTDFY RGVAGQYDEP ALTVHFRAEG RHEYTALAFV PGSKPFDLFD PDRKGRMKLY
     VKRVFITDEA ELLPRYLRFV RGLVDTADLP LNVSREMIQE SPLLANIRKG LTNRVLTSIE
     KLAESDSEAF AKIWENFGSV IKEGIYEDFE RRGQLLALSR FRTTADDDKP RALSDYVKEM
     KEGQSAIYYL TGDNLAQLKA SPQLEGFRAR GIEVLLLTCP VDSFWVTTAP DFDGKPFKSI
     TQGAADLAGI AKNDDAAAAS PEAGAAVTDF VSFARETLGE AVSDVRTSDR LTESAVCLVA
     PEQGPDRQLQ KMLQDAGRIE GAPKPVLEIN PGHQLIAALA TCPSEDKAFR EDAVKLLLDQ
     ARVLDGDRPE DPRAFAERLS RVFGRALKE
 
 
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