ID   HSCA_PSEF5              Reviewed;         620 AA.
AC   Q4K6U2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PFL_4961;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY94190.1; -; Genomic_DNA.
DR   RefSeq; WP_011063214.1; NC_004129.6.
DR   AlphaFoldDB; Q4K6U2; -.
DR   SMR; Q4K6U2; -.
DR   STRING; 220664.PFL_4961; -.
DR   EnsemblBacteria; AAY94190; AAY94190; PFL_4961.
DR   GeneID; 57477943; -.
DR   KEGG; pfl:PFL_4961; -.
DR   PATRIC; fig|220664.5.peg.5082; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_3_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000008540; 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; Reference proteome.
FT   CHAIN           1..620
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044872"
SQ   SEQUENCE   620 AA;  66212 MW;  B59F1E6B54AE024F CRC64;
     MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVAALRSGL SEPLADAQGQ VILPSAVRYH
     ADRVEVGESA RLAAPTDPLN TVLSVKRLMG RGLSDVKQLG EQLPYRFVEG ESHMPFIETI
     QGPKSPVEVS AEVLKVLRQR AEAALGGELV GAVITVPAYF DDAQRQATKD AAKLAGLNVL
     RLLNEPTAAA VAYGLDQHAE GVVAIYDLGG GTFDISILRL TGGVFEVLAT GGDTALGGDD
     FDHAIAGWII EGAGLSADLD PGTQRSLLQA ACAAKEALTG AASVEVVYGD WRATLTRDAF
     DALIEPMVAR SLKACRRAVR DSNVELDEVQ AVVMVGGSTR VPRVREAVAE MFGRQPLTEI
     DPDQVVAIGA AIQADTLAGN KREGGELLLL DVIPLSLGLE TMGGLMEKVI PRNTTIPVAR
     AQDFTTYKDG QTAMMVHVLQ GERELISDCR SLARFELRGI PPMVAGAAKI RVTFQVDADG
     LLSVSARELG SGVEASIQVK PSYGLTDGEI AKMLKDSFQY AGDDKVARVL REQQVDAQRL
     IEAVQGALDA DGERLLDAEE RMVIELQMQE LSELMRGTDG YAIEQQTKRL SQVTDAFAAR
     RLDSTVKAAL AGRNLNEIEE