HSCA_PSEAB
ID HSCA_PSEAB Reviewed; 619 AA.
AC Q02RW4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PA14_14780;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ13071.1; -; Genomic_DNA.
DR RefSeq; WP_003092822.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02RW4; -.
DR SMR; Q02RW4; -.
DR PRIDE; Q02RW4; -.
DR EnsemblBacteria; ABJ13071; ABJ13071; PA14_14780.
DR KEGG; pau:PA14_14780; -.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR BioCyc; PAER208963:G1G74-1212-MON; -.
DR Proteomes; UP000000653; 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; Stress response.
FT CHAIN 1..619
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044870"
SQ SEQUENCE 619 AA; 66460 MW; 9F1FE80E16F489B0 CRC64;
MALLQIAEPG QSPKPHERRL AVGIDLGTTN SLVAAVRSGV AEPLPDAQGR LILPSAVRYH
AERAEVGESA RAAAAKDPFN TIISVKRLMG RGLEDVKQLG EQLPYRFRQG ESHMPFIETV
QGLKSPVEVS ADILRELRQR AETTLGGELV GAVITVPAYF DDAQRQATKD AARLAGLNVL
RLLNEPTAAA VAYGLDKGAE GLVAIYDLGG GTFDISILRL TRGVFEVLAT GGDTALGGDD
FDHAIAGWVI EQAGLSADLD 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
