HSCA_PSEPF
ID HSCA_PSEPF Reviewed; 621 AA.
AC Q3K7A9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Pfl01_4608;
OS Pseudomonas fluorescens (strain Pf0-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=205922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pf0-1;
RX PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT "Genomic and genetic analyses of diversity and plant interactions of
RT Pseudomonas fluorescens.";
RL Genome Biol. 10:R51.1-R51.16(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; CP000094; ABA76345.1; -; Genomic_DNA.
DR RefSeq; WP_011335814.1; NC_007492.2.
DR AlphaFoldDB; Q3K7A9; -.
DR SMR; Q3K7A9; -.
DR STRING; 205922.Pfl01_4608; -.
DR EnsemblBacteria; ABA76345; ABA76345; Pfl01_4608.
DR KEGG; pfo:Pfl01_4608; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_6; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000002704; 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.
FT CHAIN 1..621
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044875"
SQ SEQUENCE 621 AA; 66189 MW; 69732BFBC907D280 CRC64;
MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVAALRSGL SEPLADAEGR VILPSAVRYH
ADRVEVGESA KLAASSDPLN TVLSVKRLMG RGLSDVKQLG DQLPYRFVGG ESHMPFIDTV
QGPKSPVEVS ADILKVLRQR AEATLGGELV GAVITVPAYF DDAQRQATKD AAKLAGLNVL
RLLNEPTAAA VAYGLDQHAE GLVAIYDLGG GTFDISILRL TGGVFEVLAT GGDSALGGDD
FDHAIAGWII ESASLSADLD PGAQRSLLQA ACAAKEALTD SDSVEVAYGD WKAQLTREAF
DALIEPMVAR SLKACRRAVR DSGVELEDVH AVVMVGGSTR VPRVREAVAE AFGRQPLTEI
DPDQVVAIGA AIQADTLAGN KRDGGELLLL DVIPLSLGLE TMGGLMEKVI PRNTTIPVAR
AQDFTTYKDG QSAMAIHVLQ GERELISDCR SLARFELRGI PAMVAGAAKI RVTFQVDADG
LLSVSARELG SGVEASIQVK PSYGLTDGEI AKMLKDSFQH ANDDKVARVL REQQVDAQRL
IEAVQGALEA DGERLLDAEE RMVIDLQVQE LTELMKGTDG YAIEQQTKRL SQVTDAFAAR
RMDQTVKAAL SGRNLNEIED I