HSCA_PSEU5
ID HSCA_PSEU5 Reviewed; 620 AA.
AC A4VNX8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=PST_3038;
OS Pseudomonas stutzeri (strain A1501).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=379731;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A1501;
RX PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT "Nitrogen fixation island and rhizosphere competence traits in the genome
RT of root-associated Pseudomonas stutzeri A1501.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(2008).
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; CP000304; ABP80679.1; -; Genomic_DNA.
DR RefSeq; WP_011914133.1; NC_009434.1.
DR AlphaFoldDB; A4VNX8; -.
DR SMR; A4VNX8; -.
DR STRING; 379731.PST_3038; -.
DR EnsemblBacteria; ABP80679; ABP80679; PST_3038.
DR KEGG; psa:PST_3038; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_1_6; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000000233; 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; Reference proteome;
KW Stress response.
FT CHAIN 1..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044877"
SQ SEQUENCE 620 AA; 66588 MW; 1FA04995772A5073 CRC64;
MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVAALRSGV TAPLADADGQ VILPSVVRYH
ADRVEVGACA KRAAAADPFN TISSVKRLMG RGLADVKQLG EQLPYRFRQA ESQMPFIETV
QGAKSPVEIS AEILRALRER AEAALGGELV GAVITVPAYF DDAQRQATKD AARLAGLNVL
RLLNEPTAAA VAYGLDRQAE GVVAIYDLGG GTFDISILRL TKGVFEVLAT GGDTALGGDD
FDHAVADWIL QQAGVSEDLA PGEQRELLKI ACDAKERLSV DETVQVAYAG WAGELHRETF
DALIEPLIAR SLRSCRRAVR DSGVELDEIT AVVMVGGSTR VPKVRSSVGQ LFGREPLTDI
DPDEVVAIGA AIQAETLAGN NRDGEELLLL DVIPLSLGLE TMGGLMEKII PRNTTIPVAR
AQDFTTYKDG QSAMMIHVLQ GERELISDCR SLARFELRGI PPMVAGAAKI RVTFQVDADG
LLSVSARELA SGVEASIQVK PSYGLTDGEI ARMLEDSFRK ADQDRDARAL REQLVDAQRL
LEAVEAALIA DGERLLSAEE RAAIEAQMAE LRALLDSQDV SAIERQIKRL SQITDAFAAR
RLDSTVKAAL AGRRLNDIED
