ID HSCA_BURPS Reviewed; 622 AA.
AC Q63SN5;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 96.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=BPSL2285;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH36288.1; -; Genomic_DNA.
DR RefSeq; WP_009938156.1; NZ_CP009538.1.
DR RefSeq; YP_108881.1; NC_006350.1.
DR AlphaFoldDB; Q63SN5; -.
DR SMR; Q63SN5; -.
DR STRING; 272560.BPSL2285; -.
DR KEGG; bps:BPSL2285; -.
DR PATRIC; fig|272560.51.peg.3144; -.
DR eggNOG; COG0443; Bacteria.
DR Proteomes; UP000000605; 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; 3.30.420.40; -; 2.
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 NCBIfam; TIGR01991; HscA; 1.
DR PANTHER; PTHR19375:SF176; CHAPERONE PROTEIN HSCA; 1.
DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1.
DR Pfam; PF00012; HSP70; 1.
DR PRINTS; PR00301; HEATSHOCK70.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1.
DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 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_0000078623"
SQ SEQUENCE 622 AA; 65768 MW; 77ADBBEB9C3CFE1D 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 GDDADAIDTA TKALAEGTDE
FAARRMDKSI KRALAGRKLD EI
//
