HSCA_BURP0
ID HSCA_BURP0 Reviewed; 622 AA.
AC A3NX33;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN OrderedLocusNames=BURPS1106A_2651;
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a;
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; CP000572; ABN92003.1; -; Genomic_DNA.
DR RefSeq; WP_004533931.1; NC_009076.1.
DR AlphaFoldDB; A3NX33; -.
DR SMR; A3NX33; -.
DR EnsemblBacteria; ABN92003; ABN92003; BURPS1106A_2651.
DR GeneID; 56528904; -.
DR KEGG; bpl:BURPS1106A_2651; -.
DR HOGENOM; CLU_005965_2_3_4; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000006738; Chromosome I.
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_1000044849"
SQ SEQUENCE 622 AA; 65738 MW; 77B00D30EC3CFE1D 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 QAGLEAAALA 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 GDDADAIDAA TKALAEGTDE
FAARRMDKSI KRALAGRKLD EI