ID A0A3G7UUX8_9PSED Unreviewed; 620 AA. AC A0A3G7UUX8; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 22-FEB-2023, entry version 19. DE RecName: Full=Chaperone protein HscA homolog {ECO:0000256|HAMAP-Rule:MF_00679}; GN Name=hscA {ECO:0000256|HAMAP-Rule:MF_00679}; GN ORFNames=C4K02_4855 {ECO:0000313|EMBL:AZE63187.1}; OS Pseudomonas synxantha. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=47883 {ECO:0000313|EMBL:AZE63187.1, ECO:0000313|Proteomes:UP000275641}; RN [1] {ECO:0000313|EMBL:AZE63187.1, ECO:0000313|Proteomes:UP000275641} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2-79 {ECO:0000313|EMBL:AZE63187.1, RC ECO:0000313|Proteomes:UP000275641}; RA Biessy A., Novinscak A., Blom J., Leger G., Thomashow L.S., Cazorla F.M., RA Josic D., Filion M.; RT "Diversity of phytobeneficial traits revealed by whole-genome analysis of RT worldwide-isolated phenazine-producing Pseudomonas spp."; RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP-Rule:MF_00679}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {ECO:0000256|ARBA:ARBA00007381, ECO:0000256|HAMAP-Rule:MF_00679, CC ECO:0000256|RuleBase:RU003322}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP027755; AZE63187.1; -; Genomic_DNA. DR RefSeq; WP_043046818.1; NZ_CP027755.1. DR AlphaFoldDB; A0A3G7UUX8; -. DR EnsemblBacteria; AZE63187; AZE63187; C4K02_4855. DR Proteomes; UP000275641; 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; 3.30.420.40; -; 2. 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:SF176; CHAPERONE PROTEIN HSCA; 1. DR PANTHER; PTHR19375; HEAT SHOCK PROTEIN 70KDA; 1. DR Pfam; PF00012; HSP70; 1. DR PRINTS; PR00301; HEATSHOCK70. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR SUPFAM; SSF100934; Heat shock protein 70kD (HSP70), C-terminal subdomain; 1. DR SUPFAM; SSF100920; Heat shock protein 70kD (HSP70), peptide-binding domain; 1. 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00679}; KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00679}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00679}. SQ SEQUENCE 620 AA; 66016 MW; BCCB7527E783130F CRC64; MALLQIAEPG QSPQPHQRRL AVGIDLGTTN SLVAALRSGL SEPLPDADGQ VILPSAVRYH ADRTEVGESA KMAASSDPLN TVLSVKRLMG RGLSDVKQLG DQLPYRFVGG ESHMPFIDTV QGPKSPVEVS ADILKVLRQR AETTLGGELV GAVITVPAYF DDAQRQATKD AAKLAGLNVL RLLNEPTAAA VAYGLDQHAE GLVAIYDLGG GTFDISILRL TGGVFEVLAT GGDSALGGDD FDHAIAGWII TCAGLSADLD PGAQRNLLQT ACAAKEALTD AASVEVSYGS WSAQLTREAF DALIEPMVAR SLRACRRAVR DSGVELEDVA AVVMVGGSTR VPRVREAVAE AFGRQPLTEI DPDQVVAIGA AIQADTLAGN KRDGGELLLL DVIPLSLGLE TMGGLMEKVI PRNTTIPVAR AQDFTTYKDG QTAMMIHVLQ GERELISDCR SLARFELRGI PAMVAGAAKI RVTYQVDADG LLSVAARELG SGVEASIQVK PSYGLTDGEI AKMLKDSFQY AGDDKVARVL REQQVDAQRL LEAVQGALDA DGERLLDAEE RMVIDLQMQE LAELMKGNDG YAIEQQTKRL SQVTDAFAAR RMDQTVKAAL AGRNLNEIEE //