ID A0A3G7UUX8_9PSED Unreviewed; 620 AA. AC A0A3G7UUX8; DT 13-FEB-2019, integrated into UniProtKB/TrEMBL. DT 13-FEB-2019, sequence version 1. DT 13-NOV-2019, entry version 5. 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., RA Cazorla F.M., Josic D., Filion M.; RT "Diversity of phytobeneficial traits revealed by whole-genome analysis RT of 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 CC cluster-containing proteins. Has a low intrinsic ATPase activity CC which is markedly stimulated by HscB. {ECO:0000256|HAMAP- CC Rule:MF_00679, ECO:0000256|SAAS:SAAS01158962}. CC -!- SIMILARITY: Belongs to the heat shock protein 70 family. CC {ECO:0000256|HAMAP-Rule:MF_00679, ECO:0000256|RuleBase:RU003322, CC ECO:0000256|SAAS:SAAS00561161}. 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 Proteomes; UP000275641; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051082; F:unfolded protein binding; IEA:InterPro. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule. 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; 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 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|HAMAP-Rule:MF_00679, KW ECO:0000256|RuleBase:RU003322, ECO:0000256|SAAS:SAAS00063444}; KW Chaperone {ECO:0000256|HAMAP-Rule:MF_00679, KW ECO:0000256|SAAS:SAAS00448035}; KW Complete proteome {ECO:0000313|Proteomes:UP000275641}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00679, KW ECO:0000256|RuleBase:RU003322, ECO:0000256|SAAS:SAAS00448038}. 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 //