HSCA_PSEU2
ID HSCA_PSEU2 Reviewed; 620 AA.
AC Q4ZX30;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Chaperone protein HscA homolog {ECO:0000255|HAMAP-Rule:MF_00679};
GN Name=hscA {ECO:0000255|HAMAP-Rule:MF_00679}; OrderedLocusNames=Psyr_1241;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY36292.1; -; Genomic_DNA.
DR RefSeq; WP_011266907.1; NC_007005.1.
DR RefSeq; YP_234330.1; NC_007005.1.
DR AlphaFoldDB; Q4ZX30; -.
DR SMR; Q4ZX30; -.
DR STRING; 205918.Psyr_1241; -.
DR EnsemblBacteria; AAY36292; AAY36292; Psyr_1241.
DR KEGG; psb:Psyr_1241; -.
DR PATRIC; fig|205918.7.peg.1273; -.
DR eggNOG; COG0443; Bacteria.
DR HOGENOM; CLU_005965_2_3_6; -.
DR OMA; PDPHQRR; -.
DR Proteomes; UP000000426; 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..620
FT /note="Chaperone protein HscA homolog"
FT /id="PRO_1000044876"
SQ SEQUENCE 620 AA; 66492 MW; DB4A984D88E3EE5B CRC64;
MALLQIAEPG LSPQPHQRRL AVGIDLGTTN SLVAAVRSGL SEPLADAEGQ VILPSAVRYH
ADRVEVGQSA KIAASQDPFN TVLSVKRLMG RGLTDVKQLG EQLPYRFVGG ESHMPFIDTV
QGPKSPVEVS ADILKVLRQR AEASLGGELV GAVITVPAYF DDAQRQATKD AARLAGLNVL
RLLNEPTAAA VAYGLDQKAE GVVAIYDLGG GTFDISILRL TGGVFEVLAT GGDTALGGDD
FDHAIASWIV TDAGLSADID PSAQRSLLQA ACSAKEALTD AESVEVVYGE WRGTLTREAL
NALIEPMVAR SLKACRRAVR DTGIELEEVE AVVMVGGSTR VPRVREAVAE LFGRQPLTEI
DPDQVVAIGA AIQADTLAGN KRDGGELLLL DVIPLSLGLE TMGGLMEKVI PRNTTIPVAR
GQEFTTYKDG QTAMKIHVLQ GERELISDCR SLARFELRGI PPMVAGAAKI RVTFQVDADG
LLSVSAREMG SGIESSIQVK PSYGLTDDEV TRMLKDSFEY AGDDKVARVL REHQVDAERL
LEAVQGALDA DGERLLDEEE RLVINLQMDE LRELMQGTDG YAIEQQTKRL SQVTDAFAAR
RLDSTVKAAL AGRNLNEIEE
