ID KAD6_THEVO Reviewed; 153 AA.
AC Q97B38;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 89.
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=TV0621; ORFNames=TVG0613288;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000).
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}.
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DR EMBL; BA000011; BAB59763.1; -; Genomic_DNA.
DR RefSeq; WP_010916880.1; NC_002689.2.
DR AlphaFoldDB; Q97B38; -.
DR SMR; Q97B38; -.
DR STRING; 273116.gene:9381409; -.
DR PaxDb; 273116-14324837; -.
DR GeneID; 1441728; -.
DR KEGG; tvo:TVG0613288; -.
DR eggNOG; arCOG01038; Archaea.
DR HOGENOM; CLU_079096_0_1_2; -.
DR OrthoDB; 8730at2157; -.
DR PhylomeDB; Q97B38; -.
DR Proteomes; UP000001017; Chromosome.
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 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..153
FT /note="Putative adenylate kinase"
FT /id="PRO_0000153918"
FT REGION 31..47
FT /note="NMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT REGION 94..104
FT /note="LID"
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 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 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00039"
SQ SEQUENCE 153 AA; 17439 MW; 8AF616DBD4758532 CRC64;
MGKIACITGP PGAGKSTVCS KLREYGYNCK EGNELAKEYG CLFDEEVDVE CLEEKLAEDR
FDGIICSHYS HLLGCSTVFI LEADLNDLID RMRARGYSEE KIQENIETQM SSIFYYESLE
RLPANRIFTL YNGNIDETAK RIISIIERSR NNK
//
