ID   HSCA_XENNA              Reviewed;         615 AA.
AC   Q8GLE4; D3VLM8;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=XNC1_3302;
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG
OS   1036 / NCIMB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 / AN6;
RX   PubMed=12775707; DOI=10.1128/jb.185.12.3678-3682.2003;
RA   Martens E.C., Gawronski-Salerno J., Vokal D.L., Pellitteri M.C.,
RA   Menard M.L., Goodrich-Blair H.;
RT   "Xenorhabdus nematophila requires an intact iscRSUA-hscBA-fdx operon to
RT   colonize Steinernema carpocapsae nematodes.";
RL   J. Bacteriol. 185:3678-3682(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 / AN6;
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA   Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA   Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA   Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA   Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA   Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA   Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA   van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA   Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA   Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT   convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:E27909-E27909(2011).
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; AY138456; AAN17749.1; -; Genomic_DNA.
DR   EMBL; FN667742; CBJ91354.1; -; Genomic_DNA.
DR   RefSeq; WP_013184955.1; NC_014228.1.
DR   AlphaFoldDB; Q8GLE4; -.
DR   SMR; Q8GLE4; -.
DR   STRING; 406817.XNC1_3302; -.
DR   EnsemblBacteria; CBJ91354; CBJ91354; XNC1_3302.
DR   KEGG; xne:XNC1_3302; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   Proteomes; UP000008075; 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.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..615
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_0000078656"
SQ   SEQUENCE   615 AA;  66420 MW;  FA99AAA480A59657 CRC64;
     MALLQISEPG LSAAPHQRRL AAGIDLGTTH SLVAVVRSGQ TETLADSENR HLLPSVVQYR
     KEDIQVGWQA RQQAASDPVN TVSSVKRMMG RSLADIQKRY PNLPYQFQAS ENGLPLINTA
     AGLVDPIQVS SDILKSLAQR AEKTLDGKLD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDVSILRL SRGVFEVLAT GGDTALGGDD
     FDLLLANWIR EQAGISDNDH RLQRQLLDIA TQTKIVLSEA DSAEICFADW QGRITRNEFN
     ELITSLVKRT LLSCRRALKD AGVTADEVLQ VVMVGGSTRV PLVRNMVGEF FDREPLTSID
     PDRVVAIGAA IQADILVGNK PDSEMLLLDV IPLSLGLETM GGLVEKVIPR NTTIPVARAQ
     EFTTFKDGQS AMSIHVVQGE RELVNDCRSL ARFTLRGIPP LAAGGAHIRV TFQVDADGLL
     SVSALEKSTG IESSIQVKPS YGLSDEEIAR MLKDSMTNAQ EDIQVRKLAE QKVEAARVLE
     SLTGALEKDA DLLSQEEQVA IDAAVQALIE SVQGTSPDAI ESAIKQLDKQ TQEFAARRMD
     TSIRRALAGH SVDEI