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HSCA_BURM1
ID   HSCA_BURM1              Reviewed;         622 AA.
AC   A9AGU7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN   OrderedLocusNames=Bmul_1148, BMULJ_02106;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Chaperone involved in the maturation of iron-sulfur cluster-
CC       containing proteins. Has a low intrinsic ATPase activity which is
CC       markedly stimulated by HscB. {ECO:0000255|HAMAP-Rule:MF_00679}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00679}.
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DR   EMBL; CP000868; ABX14838.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG44013.1; -; Genomic_DNA.
DR   RefSeq; WP_012213078.1; NC_010804.1.
DR   AlphaFoldDB; A9AGU7; -.
DR   SMR; A9AGU7; -.
DR   STRING; 395019.Bmul_1148; -.
DR   EnsemblBacteria; BAG44013; BAG44013; BMULJ_02106.
DR   KEGG; bmj:BMULJ_02106; -.
DR   KEGG; bmu:Bmul_1148; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_4; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000008815; Chromosome 1.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR   CDD; cd10236; HscA_like_NBD; 1.
DR   Gene3D; 1.20.1270.10; -; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   HAMAP; MF_00679; HscA; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR042039; HscA_NBD.
DR   InterPro; IPR029048; HSP70_C_sf.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   InterPro; IPR010236; ISC_FeS_clus_asmbl_HscA.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF100934; SSF100934; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
DR   TIGRFAMs; TIGR01991; HscA; 1.
DR   PROSITE; PS00297; HSP70_1; 1.
DR   PROSITE; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..622
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131669"
SQ   SEQUENCE   622 AA;  66020 MW;  C15A9E511E7AD428 CRC64;
     MALLQISEPG MAPAPHQRRL AVGIDLGTTN SLVAAVRNSV PEVLPDDAGR VLLPSVVRYL
     ENGGRRIGHD AKAQAATDPR NTIVSVKRFM GRGKAEVEGA ANAPYEFVDA PGMVQIRTVD
     GVKSPVEVSA EILATLRQRA EDTLGDELVG AVITVPAYFD DAQRQATKDA ARLAGLNVLR
     LLNEPTAAAI AYGLDNAAEG LYAVYDLGGG TFDLSILKLT KGVFEVLAAG GDSALGGDDF
     DHALFDHVLA QAGLDAKTLA PEDVRLLLDR VRVLKEALSS APEAALDVTL SNGAHLAQTI
     SHDTFATLVE PLVQRTLTPT RKALRDAQVT PADIKGVVLV GGATRMPVIR EAVAKYFGQP
     PLVNLDPDQV VALGAAIQAD LLAGNRGSGD DWLLLDVIPL SLGVETMGGL VEKIIPRNST
     IPIARAQEFT TFKDGQTAMA IHVVQGEREL VADCRSLARF ELRGIPPMTA GAARIRVTYQ
     VDADGLLSVF AREQHSGVEA SVVVKPSYGL ADDDIAKMLE DSFKTAEVDM RARALREAQV
     EAERMIEATQ AALAADGELL DAVERAEIDA RVAALRTIAQ GDDADAIEAA TKALADGTDE
     FAARRMDKSI KRALSGRRLD EI
 
 
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