ID   HSCA_BURMS              Reviewed;         622 AA.
AC   A1V5M2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN   OrderedLocusNames=BMASAVP1_A2213;
OS   Burkholderia mallei (strain SAVP1).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320388;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAVP1;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000526; ABM50174.1; -; Genomic_DNA.
DR   RefSeq; WP_004193590.1; NC_008785.1.
DR   AlphaFoldDB; A1V5M2; -.
DR   SMR; A1V5M2; -.
DR   GeneID; 56596079; -.
DR   KEGG; bmv:BMASAVP1_A2213; -.
DR   HOGENOM; CLU_005965_2_1_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_1000044848"
SQ   SEQUENCE   622 AA;  65796 MW;  0BC00B046BD30367 CRC64;
     MALLQISEPG MAPAPHQRRL AVGIDLGTTN SLVAAVRNSI PEALPDDAGR VLLPSVVRYL
     DKGGRRIGHA AKEEAAIDPR NTIVSVKRFM GRGKAEVEGA ANAPYEFVDA PGMVQIRTVD
     GVKSPVEVSA EILATLRQRA EDTLGDDLVG AVITVPAYFD DAQRQATKDA ARLAGLNVLR
     LLNEPTAAAI AYGLDNGAEG LYAVYDLGGG TFDLSILKLT KGVFEVLAAG GDSALGGDDF
     DHLLFEHVLA QAGLEVAALA PEDVRLLLDR VRGAKEALSA APQARVDVKL STGEKLAQTI
     TRDTFAALVE PLVQRTLGPT RKALRDAQVS AADIKGVVLV GGATRMPVIR DAVAKYFGQP
     PLVNLDPDQV VALGAAIQAD LLAGNRSGGD DWLLLDVIPL SLGVETMGGL VEKIIPRNST
     IPVARAQEFT TFKDGQTAMA IHVVQGEREL VSDCRSLARF ELRGIPPMTA GAARIRVTYQ
     VDADGLLSVF AREQHSGVEA SVVVKPSYGL GDDDIARMLE DSFKTAEVDM RARALREAQV
     EAQRLVEATE AALVADGDLL DASERATVDA LVASLRALAP GDDADAIDTA TKALAEGTDE
     FAARRMDKSI KRALAGRKLD EI