ID   HSCA_PSEA8              Reviewed;         619 AA.
AC   B7UWI1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN   Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PLES_11641;
OS   Pseudomonas aeruginosa (strain LESB58).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=557722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LESB58;
RX   PubMed=19047519; DOI=10.1101/gr.086082.108;
RA   Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I.,
RA   Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A.,
RA   Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D.,
RA   Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.;
RT   "Newly introduced genomic prophage islands are critical determinants of in
RT   vivo competitiveness in the Liverpool epidemic strain of Pseudomonas
RT   aeruginosa.";
RL   Genome Res. 19:12-23(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; FM209186; CAW25891.1; -; Genomic_DNA.
DR   RefSeq; WP_012613648.1; NC_011770.1.
DR   AlphaFoldDB; B7UWI1; -.
DR   SMR; B7UWI1; -.
DR   PRIDE; B7UWI1; -.
DR   KEGG; pag:PLES_11641; -.
DR   HOGENOM; CLU_005965_2_1_6; -.
DR   OMA; PDPHQRR; -.
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; Stress response.
FT   CHAIN           1..619
FT                   /note="Chaperone protein HscA homolog"
FT                   /id="PRO_1000131684"
SQ   SEQUENCE   619 AA;  66447 MW;  9FBFF34CD83249B0 CRC64;
     MALLQIAEPG QSPKPHERRL AVGIDLGTTN SLVAAVRSGV AEPLPDAQGR LILPSAVRYH
     AERAEVGESA RAAAAEDPFN TVISVKRLMG RGLEDVKQLG EQLPYRFRQG ESHMPFIETV
     QGLKSPVEVS ADILRELRQR AETTLGGELV GAVITVPAYF DDAQRQATKD AARLAGLNVL
     RLLNEPTAAA VAYGLDKGAE GLVAIYDLGG GTFDISILRL TRGVFEVLAT GGDTALGGDD
     FDHAIAGWVI EEAGLSADLD PGSQRQLLQI ACAAKERLTD EASVRVAYGD WSGELSRATL
     DELIEPFVAR SLKSCRRAVR DSGVDLEEIR SVVMVGGSTR VPRVRTAVGE LFGCEPLTDI
     DPDQVVAIGA AIQADALAGN KRGEELLLLD VIPLSLGLET MGGLMEKVIP RNTTIPVARA
     QEFTTYKDGQ TAMMIHVLQG ERELVKDCRS LARFELRGIP PMVAGAAKIR VTFQVDADGL
     LGVSARELSS GVEASIQVKP SYGLTDGEIA RMLKDSFDYA GDDKAARALR EQQVEAQRLL
     EAVQSALDVD GERLLDEEER LAIAAQMDTL RELAGGSDTA AIENQIKRLS QVTDAFAARR
     MDATVKAALS GRRLNEIEE