ID P47K_PSECL Reviewed; 419 AA. AC P31521; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1993, sequence version 1. DT 03-MAY-2023, entry version 63. DE RecName: Full=Zinc chaperone P47K; DE EC=3.6.5.- {ECO:0000250|UniProtKB:P24203}; DE AltName: Full=47 kDa protein {ECO:0000303|PubMed:2013568}; DE Short=P47K {ECO:0000303|PubMed:2013568}; OS Pseudomonas chlororaphis (Pseudomonas aureofaciens). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=B23; RX PubMed=2013568; DOI=10.1128/jb.173.8.2465-2472.1991; RA Nishiyama M., Horinouchi S., Kobayashi M., Nagasawa T., Yamada H., RA Beppu T.; RT "Cloning and characterization of genes responsible for metabolism of RT nitrile compounds from Pseudomonas chlororaphis B23."; RL J. Bacteriol. 173:2465-2472(1991). CC -!- FUNCTION: Zinc chaperone that directly transfers zinc cofactor to CC target proteins, thereby activating them. Zinc is transferred from the CC CXCC motif in the GTPase domain to the zinc binding site in target CC proteins in a process requiring GTP hydrolysis. CC {ECO:0000250|UniProtKB:Q8VEH6}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; CC Evidence={ECO:0000250|UniProtKB:P24203}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000250|UniProtKB:P24203}; CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1 CC subfamily. {ECO:0000305}. 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; D90216; BAA14247.1; -; Genomic_DNA. DR PIR; D42725; D42725. DR AlphaFoldDB; P31521; -. DR SMR; P31521; -. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR CDD; cd03112; CobW-like; 1. DR Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR036627; CobW-likC_sf. DR InterPro; IPR011629; CobW-like_C. DR InterPro; IPR003495; CobW/HypB/UreG_dom. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR43603; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1. DR PANTHER; PTHR43603:SF1; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1. DR Pfam; PF02492; cobW; 1. DR Pfam; PF07683; CobW_C; 1. DR SMART; SM00833; CobW_C; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Hydrolase; Nucleotide-binding. FT CHAIN 1..419 FT /note="Zinc chaperone P47K" FT /id="PRO_0000058140" FT DOMAIN 262..379 FT /note="CobW C-terminal" FT MOTIF 76..79 FT /note="CXCC motif" FT /evidence="ECO:0000255" FT BINDING 17..24 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 79..83 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" FT BINDING 187..190 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000255" SQ SEQUENCE 419 AA; 46666 MW; FF5113800E27FF0C CRC64; MIEGAQAGRL PVTVLSGFLG AGKTTLLNAI LRNRQGLRVA VIVNDMSEVN LDAESVQRDV SLHRGRDELI EMSNGCICCT LRADLLEQIS DLARQQRFDY LLIESTGISE PMPVAETFAF LDTEGFSLSE LARLDTLVTV VDGSQFQALL ESTDTVARAD TEAHTSTRHL ADLLIEQVEY ANVILVNKRD LIDEPGYQAV HAILAGLNPS ARIMPMAHGN VALSSLLDTH LFDLPSLAAS PGWMRKMEAT DTPASESDTY GVTSWVYRER APFHPQRLLE FLQKPWHNGR LLRSKGYFWL ASRHLEIGLL AQSGKQFQWD YVGRWWNFIE PSQWPRDEYR LQGIMAKWDS VVGDCRQELV FIGQGLDTRV LQRELDHCLL SAQEIAAGPL AWQALPAATA FDTEALSARP TPPMAVQPT //