HSCA_BURCJ
ID HSCA_BURCJ Reviewed; 622 AA.
AC B4EDS3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679};
GN OrderedLocusNames=BceJ2315_21570; ORFNames=BCAL2194;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
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; AM747720; CAR52495.1; -; Genomic_DNA.
DR RefSeq; WP_006481972.1; NC_011000.1.
DR AlphaFoldDB; B4EDS3; -.
DR SMR; B4EDS3; -.
DR STRING; 216591.BCAL2194; -.
DR EnsemblBacteria; CAR52495; CAR52495; BCAL2194.
DR KEGG; bcj:BCAL2194; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_4; -.
DR OMA; PDPHQRR; -.
DR OrthoDB; 161217at2; -.
DR BioCyc; BCEN216591:G1G1V-2409-MON; -.
DR Proteomes; UP000001035; 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_1000131668"
SQ SEQUENCE 622 AA; 66060 MW; B5C5943FB7339DE9 CRC64;
MALLQISEPG MAPAPHQRRL AVGIDLGTTN SLVAAVRNSV PEVLPDEAGR VLLPSVVRYL
EKGGRRIGHE AKEQAATDPR NTIVSVKRFM GRGKAEVEGA ANAPYEFVDA PGMVQIRTID
GVKSPVEVSA EILATLRYRA EDTLGDELVG AVITVPAYFD DAQRQATKDA ARLAGLNVLR
LLNEPTAAAI AYGLDNAAEG LYAVYDLGGG TFDLSILKLT KGVFEVLAAG GDSALGGDDF
DHALFDHVLA QAGIDAKTLA PEDVRLLLDR VRVLKEALSS APEAALDVTL SSGAHLAPTI
SHDTFASLVE PLVQRTLTPT RKALRDAQVT PADIKGVVLV GGATRMPVIR DAVAKYFGQP
PLVNLDPDQV VALGAAIQAD LLAGNRGTGD DWLLLDVIPL SLGVETMGGL VEKIIPRNST
IPIARAQEFT TFKDGQTAMA IHVVQGEREL VADCRSLARF ELRGIPPMTA GAARIRVTYQ
VDADGLLSVF AREQQSGVEA SVVVKPSYGL ADDDIAKMLE DSFKTAEIDM RARALREAQV
EAQRMLEATQ AALAADGELL DADERAQVDA LADALRAVAQ GDDTNAIEAA TKALADGTDE
FAARRMDKSI KRALSGRRLD EI