ID   HSCA_PHOLL              Reviewed;         616 AA.
AC   Q7N228;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=plu3279;
OS   Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS   TT01).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Photorhabdus.
OX   NCBI_TaxID=243265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15139 / CIP 105565 / TT01;
RX   PubMed=14528314; DOI=10.1038/nbt886;
RA   Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA   Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA   Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA   Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA   Glaser P., Boemare N., Danchin A., Kunst F.;
RT   "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT   luminescens.";
RL   Nat. Biotechnol. 21:1307-1313(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.
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; BX571870; CAE15653.1; -; Genomic_DNA.
DR   RefSeq; WP_011147474.1; NC_005126.1.
DR   AlphaFoldDB; Q7N228; -.
DR   SMR; Q7N228; -.
DR   STRING; 243265.plu3279; -.
DR   EnsemblBacteria; CAE15653; CAE15653; plu3279.
DR   GeneID; 24169903; -.
DR   KEGG; plu:plu3279; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   BioCyc; PLUM243265:PLU_RS16325-MON; -.
DR   Proteomes; UP000002514; 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..616
FT                   /note="Chaperone protein HscA"
FT                   /id="PRO_0000078637"
SQ   SEQUENCE   616 AA;  66544 MW;  A4305B3100B655BA CRC64;
     MALLQISEPG LSAAPHQRRL AVGIDLGTTH SLVATVRSGQ AETLMDSEER YLLPSVVRYH
     EKGPEIGWLA RQQAAYDPAN TISSVKRMMG RSLADIQQRY PNLPYQFQAS ENGLPLINTA
     TGLVDPIQVS SDILKSLVQR AEETLDGKLD GVVITVPAYF DDAQRQGTKD AARLAGLHVL
     RLLNEPTAAA IAYGLDSGQE GVIAVYDLGG GTFDVSILRL SRGVFEVLAT GGDTALGGDD
     FDLILADWIR EQAGIGSRDD HSLQRQLLDM ATQVKIALSD ADIAEINIAG WQGKITRCEF
     EALITPLIKR TLLASRRALK DAEVSADEVL QVVMVGGSTR VPLVRHRVGE FFGREPLTSI
     DPDKVVAVGA SIQADILVGN KPDSDMLLLD VIPLSLGLET MGGLVEKIIP RNTTIPVAKA
     QEFTTFKDGQ SAMSIHVVQG ERELVSDCRS LARFTLRGIP PLPAGGAHIR VTFQVDADGL
     LNVSALEKST GVEAFIQVKP SYGLSDEEIA RMIKDSMANA QEDINARQLA EQKVEAARVL
     ESVTSALEKD ADLLNEQEQA AIDAAVETLI TSVQGNDPEI IENAIKQLDK QTQEFAARRM
     DSSIRRALAG HSVDEI