ID   HSCA_BUCA5              Reviewed;         611 AA.
AC   B8D8G2;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Chaperone protein HscA {ECO:0000255|HAMAP-Rule:MF_00679};
DE   AltName: Full=Hsc66 {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=BUAP5A_597;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=563178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5A;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(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. Involved in the maturation of IscU.
CC       {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; CP001161; ACL30938.1; -; Genomic_DNA.
DR   RefSeq; WP_009874552.1; NC_011833.1.
DR   AlphaFoldDB; B8D8G2; -.
DR   SMR; B8D8G2; -.
DR   KEGG; bap:BUAP5A_597; -.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; IRVEVTF; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000006904; Chromosome.
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; Stress response.
FT   CHAIN           1..611
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_1000147711"
SQ   SEQUENCE   611 AA;  69837 MW;  32B567C53073082A CRC64;
     MIFFKKKHDK KLLLGIDLGT TYSLAATVRE KSVILLLDKK KRYLLPSVVH YKKNKISVGW
     KALENITEDP TNTISSVKRL LGRSINFVKK KFPILPYLIE KDIHEGIFFR TNFGNITPID
     VSSHILKKLK KRAVLLFNQE IDASVITVPA YFNDFQKKET KKAAVLSGIN LIRLLNEPTA
     AAVAYGLQKL KKGIVLVYDL GGGTFDVSIL NLNKGIFEVL ATSGDSNLGG DDFDDALAKN
     IYKKSNLQNR CNDFFQTSLL QIAKSTKLKL TKYEKVEVHF FDWKGYITRE EFNLIIIDFI
     KKTLFICSDL LEEINLSVEQ IKEVIMVGGS TRIPLVHTEV SKFFKKDLLK SINPDQVVAI
     GAAMHVDMLF SSKNNTKNKV ILLDVMPLSL GIEVMGGFVE KIIFRNTSLP ISKTKEFTTY
     KDNQTSILIH IVQGERELVK DCISLSRFVL RDIKPQKAGL VRILVTFQVD TDGLIHVKIL
     ENYSSKEKKI IIDNNITLKN LNISQILKDS LKHSKDDYYF RVKEEKKIEC VRTLEILNKS
     LKKHLKLISK KELKKIKYTQ EKLQKSIQED DYFSMKNNLQ KLDEVSKNFF SLQLKNAIDC
     SSIKNILKEN I