ID   HSCA_BUCBP              Reviewed;         511 AA.
AC   Q89A16;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Chaperone protein HscA;
GN   Name=hscA; OrderedLocusNames=bbp_547;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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. Involved in the maturation of IscU (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family. {ECO:0000305}.
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DR   EMBL; AE016826; AAO27245.1; -; Genomic_DNA.
DR   RefSeq; WP_011091646.1; NC_004545.1.
DR   AlphaFoldDB; Q89A16; -.
DR   SMR; Q89A16; -.
DR   STRING; 224915.bbp_547; -.
DR   PRIDE; Q89A16; -.
DR   EnsemblBacteria; AAO27245; AAO27245; bbp_547.
DR   GeneID; 56471081; -.
DR   KEGG; bab:bbp_547; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_0_0_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   CDD; cd10236; HscA_like_NBD; 1.
DR   Gene3D; 2.60.34.10; -; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR042039; HscA_NBD.
DR   InterPro; IPR029047; HSP70_peptide-bd_sf.
DR   InterPro; IPR013126; Hsp_70_fam.
DR   PANTHER; PTHR19375; PTHR19375; 1.
DR   Pfam; PF00012; HSP70; 1.
DR   SUPFAM; SSF100920; SSF100920; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
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..511
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_0000078621"
SQ   SEQUENCE   511 AA;  57609 MW;  B9AB517FB4DA1529 CRC64;
     MITLKTIKKK YNIEQKNTKL SIGIDFGTTY SLVASALEDN IYIILDQNNR ALLPSIINYT
     SKKPIVGWEA QKQAINDPKN TIISIKRLIG HSYDEINKLY PNLPYHLTYD KNGILSFIVQ
     DNLINTINVS SEIFKTLKNR VNTIFNQKIL GAVITVPAHF NDLQRQEIKK SAELANLNII
     RLLNEPTSAA IAYGLHLNKN KIVAIYDLGG GTFDISILKL NQGIFEVLAT SGNTNLGGDD
     FDQLLVNYIQ KKTHFSYSKL DFIFQRKLLY LAKSIKIKLT SHNSVQFQFN NSKMHTITRF
     EFEKMIEPLI LKTLNICQHV LHDSNTNLTH IEEIILVGGS TNIPIVQRKV SDFFKQLPLC
     TINPEQVVVA GAAIQANMLT NGSKYNNFIL LDVVPLSLGI EVIGNIVEKI ILKNTPLPIS
     KTKTFTTFKD KQTTMLIHVL QGEHKLVNKC QSLCRFVLKE IPKKPAGKII VLVNFQIDVN
     GLLSVTAEIK STKIRKNITV NASIPIKKYR N