HSCA_BURL3
ID HSCA_BURL3 Reviewed; 622 AA.
AC Q39EU4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN OrderedLocusNames=Bcep18194_A5428;
OS Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS R18194 / 383).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=482957;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia sp. 383.";
RL Submitted (OCT-2005) 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; CP000151; ABB09022.1; -; Genomic_DNA.
DR RefSeq; WP_011352559.1; NC_007510.1.
DR AlphaFoldDB; Q39EU4; -.
DR SMR; Q39EU4; -.
DR EnsemblBacteria; ABB09022; ABB09022; Bcep18194_A5428.
DR GeneID; 45095308; -.
DR KEGG; bur:Bcep18194_A5428; -.
DR PATRIC; fig|482957.22.peg.2381; -.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR Proteomes; UP000002705; 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.
FT CHAIN 1..622
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044852"
SQ SEQUENCE 622 AA; 66068 MW; BDD033A7D95FDF3A CRC64;
MALLQISEPG MAPAPHQRRL AVGIDLGTTN SLVAAVRNSV PEVLPDEAGR VLLPSVVRYL
EKGGRRIGHE AKEQAATDPR NTIVSVKRFM GRGKAEVEGA ANAPYEFVDA PGMVQIRTID
GVKSPVEVSA EILATLRYRA EDSLGDDLVG AVITVPAYFD EAQRQATKDA ARLAGLNVLR
LLNEPTAAAI AYGLDNGSEG LYAVYDLGGG TFDLSILKLT KGVFEVLAAG GDSALGGDDF
DHALFGHVLA QAGIDVKTLA PEDVRLLLDR VRVLKEALSS APQASLDVTL SGGAHLVQTI
SHDTFASLVE PLVQRTLTPT RKALRDAQVT SADIKGVVLV GGATRMPVIR DAVAKYFGQP
PLVNLDPDQV VALGAAIQAD LLAGNRGTGD DWLLLDVIPL SLGVETMGGL VEKIIPRNST
IPIARAQEFT TFKDGQTAMA IHVVQGEREL VADCRSLARF ELRGIPPMTA GAARIRVTYQ
VDADGLLSVF AREQLSGVEA SVVVKPSYGL ADDDIAKMLE DSFKTAEIDM RARALREAQV
EAERMLEATQ AALAADGELL DADERTQVDT LAAALRAVAQ GDDTNAIEAA TKALAEGTDE
FAARRMDKSI KRALSGRRLD EI
