ID   HSCA_BUCAP              Reviewed;         609 AA.
AC   O51883;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2002, sequence version 2.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=Chaperone protein HscA;
GN   Name=hscA; OrderedLocusNames=BUsg_580;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9516544; DOI=10.1007/pl00006760;
RA   Clark M.A., Baumann L., Baumann P.;
RT   "Sequence analysis of a 34.7-kb DNA segment from the genome of Buchnera
RT   aphidicola (endosymbiont of aphids) containing groEL, dnaA, the atp operon,
RT   gidA, and rho.";
RL   Curr. Microbiol. 36:158-163(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AF008210; AAC38121.1; -; Genomic_DNA.
DR   EMBL; AE013218; AAM68114.1; -; Genomic_DNA.
DR   RefSeq; WP_011054080.1; NC_004061.1.
DR   AlphaFoldDB; O51883; -.
DR   SMR; O51883; -.
DR   STRING; 198804.BUsg_580; -.
DR   EnsemblBacteria; AAM68114; AAM68114; BUsg_580.
DR   KEGG; bas:BUsg_580; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_4_6; -.
DR   OMA; IRVEVTF; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000000416; 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   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; 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; PS00329; HSP70_2; 1.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding.
FT   CHAIN           1..609
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_0000078620"
FT   CONFLICT        342
FT                   /note="K -> N (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        344..345
FT                   /note="FR -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   609 AA;  69505 MW;  8BC662CAC7F2186D CRC64;
     MVFLKNKVKK KLILGIDFGT TYSLLASVQN ERVVLLTDDK KRYLLPSIVN FNKKKPLIGW
     EAEKKIIKDP INTITSVKRL IGRSIDFIKK EFPILPYVIE DNKDGGILFH TNSGLVTPID
     VTSEILKFLK EKSCEFFNKK IDATVITVPA YFDNLQRDSI KKAAISAKIN LIRLLNEPTS
     AAVAYGLQLN TEGLVVVYDL GGGTFDISVL KLNKGIFEVL GTAGHANLGG DDFDTLLSKY
     IYKKLNLSNQ CDNFFQSLLL KKAKEIKIKL TKYEKVEVNF FNWKGIIFRD EFNLIIKDLI
     QKTLFICSNL LKEIDLKIES IKEVIMVGGS TRVPLVYQEV KKFFRKSPLI SINPDQVVAI
     GAAIQSDMLM KNTIQKRTIL LDVTPLSLGI EVMGGFVEKI IFRNTPIPIS KTKEFTTAKD
     NQTIIVIHIL QGERELVKDC ISLSRFILKD IPSKKAGVVR ILVTFEIDTD GLISVKILEK
     FSHKEKKIQI ENVTFLQNKN IHKIIKESTI NAKEDYYLRV RKEKKIESKY ILDLLNNALQ
     EDRNLITSEE LKKIKSHQIK LQKSIDEDDF FSMKLNLKKL EEVSKNFLSL RLKKNMDSFS
     IKNLSDEIT