ID   HSCA_BURCA              Reviewed;         622 AA.
AC   Q1BHT5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Bcen_5955;
OS   Burkholderia cenocepacia (strain AU 1054).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=331271;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU 1054;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K.,
RA   Tiedje J.M., Richardson P.;
RT   "Complete sequence of chromosome 3 of Burkholderia cenocepacia AU 1054.";
RL   Submitted (MAY-2006) 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; CP000380; ABF80820.1; -; Genomic_DNA.
DR   RefSeq; WP_011549463.1; NC_008062.1.
DR   AlphaFoldDB; Q1BHT5; -.
DR   SMR; Q1BHT5; -.
DR   EnsemblBacteria; ABF80820; ABF80820; Bcen_5955.
DR   KEGG; bcn:Bcen_5955; -.
DR   HOGENOM; CLU_005965_2_4_4; -.
DR   OMA; PDPHQRR; -.
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_1000044843"
SQ   SEQUENCE   622 AA;  66019 MW;  5750E942D86E1B51 CRC64;
     MALLQISEPG MAPAPHQRRL AVGIDLGTTN SLVAAVRNSV PEVLPDEAGR VLLPSVVRYL
     EKGGRRIGHE AKEQAATDPR NTIVSVKRFM GRGKAEVEGA ANAPYEFVDA PGMVQIRTID
     GVKSPVEVSA EILATLRYRA EDSLGDDLVG AVITVPAYFD DAQRQATKDA ARLAGLNVLR
     LLNEPTAAAI AYGLDNAAEG LYAVYDLGGG TFDLSILKLT KGVFEVLAAG GDSALGGDDF
     DHALFGHVLA QAGIDAKTLA PEDVRLLLDR VRVLKEALSS APEAALDVTL SSGAHLVQTI
     SHDTFASLVE PLVQRTLTPT RKALRDAQVT PADIKGVVLV GGATRMPVIR DAVAKYFGQP
     PLVNLDPDQV VALGAAIQAD LLAGNRGTGD DWLLLDVIPL SLGVETMGGL VEKIIPRNST
     IPIARAQEFT TFKDGQTAMA IHVVQGEREL VADCRSLARF ELRGIPPMTA GAARIRVTYQ
     VDADGLLSVF AREQLSGVEA SVVVKPSYGL ADDDIAKMLE DSFKTAEIDM RARALREAQV
     EAERMLEATQ AALAADGELL ETDERAQVDA LAAALRAVAQ GDDTNAIEAA TKALADGTDE
     FAARRMDKSI KRALSGRRLD EI