ID   HSCA_PSEPK              Reviewed;         620 AA.
AC   Q88PK4;
DT   19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PP_0846;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(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. {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; AE015451; AAN66471.1; -; Genomic_DNA.
DR   RefSeq; NP_743007.1; NC_002947.4.
DR   RefSeq; WP_010952066.1; NC_002947.4.
DR   AlphaFoldDB; Q88PK4; -.
DR   SMR; Q88PK4; -.
DR   STRING; 160488.PP_0846; -.
DR   PRIDE; Q88PK4; -.
DR   EnsemblBacteria; AAN66471; AAN66471; PP_0846.
DR   KEGG; ppu:PP_0846; -.
DR   PATRIC; fig|160488.4.peg.906; -.
DR   eggNOG; COG0443; Bacteria.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   PhylomeDB; Q88PK4; -.
DR   BioCyc; PPUT160488:G1G01-921-MON; -.
DR   Proteomes; UP000000556; 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_0000078640"
SQ   SEQUENCE   620 AA;  65889 MW;  FF6707A439D15F6A CRC64;
     MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SMVAALRSGR SEPLPDAQGN VILPSAVRYL
     EGRNEVGQAA RDAASSDPLN TVLSVKRLMG RGLADVKQLG EQLPYRFVGG ESHMPFIDTV
     QGPKSPVEVS ADILKVLRER AEATLGGELV GAVITVPAYF DDAQRQATKD AARLAGLNVL
     RLLNEPTAAA VAYGLDQNAE GVVAIYDLGG GTFDISILRL TAGVFEVLAT GGDTALGGDD
     FDHAIAGWII EQAGLSSDLD PATQRALLQT ACAAKEALTD ADVVSVSHGA WHGELTRNAF
     EAMIEPLVAR SLKACRRAVR DSGVELEEVS AVVMVGGSTR VPRVREAVGA LFGRTPLTSI
     DPDQVVAIGA AIQADTLAGN RREGGELLLL DVIPLSLGLE TMGGLMEKVI PRNTTIPVAR
     AQEFTTYKDG QSAMMIHVLQ GERELISDCR SLARFELRGI PAMVAGAAKI RVTFQVDADG
     LLSVAARELG SGVEASIQVK PSYGLTDGEI ARMLKDSFEH AGSDKHARQL REHQVDGERL
     LEAVQGALDA DGDRLLSSDE RDAIEFQMQE LRDLLAGTDG AAIEQQTKRL SQVTDAFAAR
     RLDSTVKAAL AGRNLNEIEE