ID KAD6_METBF Reviewed; 182 AA. AC Q46FV0; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 29-MAY-2024, entry version 92. DE RecName: Full=Putative adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00039}; DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00039}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00039}; DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00039}; GN OrderedLocusNames=Mbar_A0258; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fusaro / DSM 804; RX PubMed=16980466; DOI=10.1128/jb.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(2006). CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase that CC catalyzes the reversible transfer of the terminal phosphate group CC between nucleoside triphosphates and monophosphates. Has also ATPase CC activity. Involved in the late maturation steps of the 30S ribosomal CC particles, specifically 16S rRNA maturation. While NMP activity is not CC required for ribosome maturation, ATPase activity is. Associates CC transiently with small ribosomal subunit protein uS11. ATP hydrolysis CC breaks the interaction with uS11. May temporarily remove uS11 from the CC ribosome to enable a conformational change of the ribosomal RNA that is CC needed for the final maturation step of the small ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00039}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00039}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00039}; CC -!- SUBUNIT: Interacts with uS11. Not a structural component of 40S pre- CC ribosomes, but transiently interacts with them by binding to uS11. CC {ECO:0000255|HAMAP-Rule:MF_00039}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00039}. 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; CP000099; AAZ69242.1; -; Genomic_DNA. DR AlphaFoldDB; Q46FV0; -. DR SMR; Q46FV0; -. DR STRING; 269797.Mbar_A0258; -. DR PaxDb; 269797-Mbar_A0258; -. DR KEGG; mba:Mbar_A0258; -. DR eggNOG; arCOG01038; Archaea. DR HOGENOM; CLU_079096_0_1_2; -. DR OrthoDB; 8730at2157; -. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1. DR InterPro; IPR020618; Adenyl_kinase_AK6. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR12595:SF0; ADENYLATE KINASE ISOENZYME 6; 1. DR PANTHER; PTHR12595; POS9-ACTIVATING FACTOR FAP7-RELATED; 1. DR Pfam; PF13238; AAA_18; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. PE 3: Inferred from homology; KW ATP-binding; Kinase; Nucleotide-binding; Ribosome biogenesis; KW rRNA processing; Transferase. FT CHAIN 1..182 FT /note="Putative adenylate kinase" FT /id="PRO_1000003091" FT REGION 30..53 FT /note="NMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT REGION 104..114 FT /note="LID" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 10 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 12 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 13 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 14 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 105 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" FT BINDING 143 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039" SQ SEQUENCE 182 AA; 21069 MW; 6EE6678F65AE38CA CRC64; MLIGLTGTPG TGKTSVSKFL ERKRHWKVIH LNEMIKEEHL YTEVDEVRDA VIADMELVRQ RLEEIIGGKE NEVIILESHL AHYIADIVII LRVYPPELKM RLKARGYSEE KIRENIEAEA LDVILVEAFE WCKKVFEINT TGKSIEETEQ HIEKIIDHIL SGNEEELPEY KPGSIDWIDL VP //