ID   HSCA_PSEFS              Reviewed;         620 AA.
AC   C3K1M1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PFLU_5064;
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(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. {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; AM181176; CAY52058.1; -; Genomic_DNA.
DR   RefSeq; WP_015885744.1; NC_012660.1.
DR   AlphaFoldDB; C3K1M1; -.
DR   SMR; C3K1M1; -.
DR   STRING; 294.SRM1_04652; -.
DR   PRIDE; C3K1M1; -.
DR   EnsemblBacteria; CAY52058; CAY52058; PFLU_5064.
DR   KEGG; pfs:PFLU_5064; -.
DR   PATRIC; fig|216595.4.peg.5199; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000002332; 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; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Chaperone; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000212531"
SQ   SEQUENCE   620 AA;  65937 MW;  9004B23EE7B51F65 CRC64;
     MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVAALRSGL SEPLPDADGQ VILPSAVRYH
     ADRTEVGESA KLAASADPLN TVLSVKRLMG RGLSDVKQLG DQLPYRFVGG ESHMPFIDTV
     QGPKSPVEVS ADILKVLRQR AETTLGGELV GAVITVPAYF DDAQRQATKD AAKLAGLNVL
     RLLNEPTAAA VAYGLDQHAE GLVAIYDLGG GTFDISILRL TGGVFEVLAT GGDSALGGDD
     FDHTVAGWII SSAGLSADLD PGAQRNLLQT ACAAKEALTD AATVEVSYGT WSAQLTREAF
     DALIEPMVAR SLKACRRAVR DSGVELEDVG AVVMVGGSTR VPRVRDAVAE AFGRQPLTEI
     DPDQVVAIGA AIQADTLAGN KRDGGELLLL DVIPLSLGLE TMGGLMEKVI PRNTTIPVAR
     AQDFTTYKDG QTAMMIHVLQ GERELISDCR SLARFELRGI PAMVAGAAKI RVTYQVDADG
     LLSVAARELA SGVEASIQVK PSYGLTDGEI AKMLKDSFQY AGDDKVARVL REQQVDAQRL
     LEAVQGALDV DGERLLDAEE RMVIDLQMQE LAELIKGTDG YAIEQQTKRL SQVTDAFAAR
     RMDQSVKAAL AGRNLNELEE