ID   HSCA_PSEA7              Reviewed;         619 AA.
AC   A6V0V2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PSPA7_1303;
OS   Pseudomonas aeruginosa (strain PA7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=381754;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA7;
RA   Dodson R.J., Harkins D., Paulsen I.T.;
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000744; ABR85726.1; -; Genomic_DNA.
DR   RefSeq; WP_012074556.1; NC_009656.1.
DR   AlphaFoldDB; A6V0V2; -.
DR   SMR; A6V0V2; -.
DR   EnsemblBacteria; ABR85726; ABR85726; PSPA7_1303.
DR   KEGG; pap:PSPA7_1303; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
DR   OrthoDB; 161217at2; -.
DR   Proteomes; UP000001582; 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.
FT   CHAIN           1..619
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000044869"
SQ   SEQUENCE   619 AA;  66462 MW;  D845B3E0FDE1D6B4 CRC64;
     MALLQIAEPG QSPKPHERRL AVGIDLGTTN SLVAAVRSGV AEPLPDARGR LILPSAVRYH
     ADRAEVGEGA RAAAAQDPLN TIISVKRLMG RGLEDVKQLG EQLPYRFRQG ESHMPFIETV
     QGLKSPVEVS ADILRELRQR AETTLGGELV GAVITVPAYF DDAQRQATKD AARLAGLNVL
     RLLNEPTAAA VAYGLDKGAE GLVAIYDLGG GTFDISILRL TRGVFEVLAT GGDTALGGDD
     FDHAVAGWVI EQAGLSADLD PGRQRELLQI ACAAKERLTD ATSVSVSYGD WRGELSRAKL
     DELIEPFIAR SLRSCRRAVR DSGIDLEEIR SVVMVGGSTR VPRVRSAVGE LFGCEPLTDI
     DPDQVVAIGA AIQADALAGN KRGEELLLLD VIPLSLGLET MGGLMEKVIP RNTTIPVARA
     QEFTTYKDGQ TAMMIHVLQG ERELVKDCRS LARFELRGIP PMVAGAAKIR VTFQVDADGL
     LGVSARELSS GVEASIQVKP SYGLTDGEIA RMLKDSFDYA GDDKAARALR EQQVEAQRLL
     EAVQSALDAD GERLLDEEEH LAIAAQMDSL RELAGGSDTA AIENQIKRLS QVTDAFAARR
     MDATVKAALS GRRLNEIEE