ID   KAD_STACA               Reviewed;          40 AA.
AC   P35141;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Adenylate kinase;
DE            Short=AK;
DE            EC=2.7.4.3;
DE   AltName: Full=ATP-AMP transphosphorylase;
DE   AltName: Full=ATP:AMP phosphotransferase;
DE   AltName: Full=Adenylate monophosphate kinase;
DE   Flags: Fragment;
GN   Name=adk;
OS   Staphylococcus carnosus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1281;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1435726; DOI=10.1007/bf00286192;
RA   Tschauder S., Driessen A.J.M., Freudl R.;
RT   "Cloning and molecular characterization of the secY genes from Bacillus
RT   licheniformis and Staphylococcus carnosus: comparative analysis of nine
RT   members of the SecY family.";
RL   Mol. Gen. Genet. 235:147-152(1992).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       group between ATP and AMP. Plays an important role in cellular energy
CC       homeostasis and in adenine nucleotide metabolism.
CC       {ECO:0000250|UniProtKB:P69441}.
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:0000250|UniProtKB:P69441};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from ADP: step 1/1. {ECO:0000250|UniProtKB:P69441}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P69441}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P69441}.
CC   -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC       small peripheral domains, NMPbind and LID, which undergo movements
CC       during catalysis. The LID domain closes over the site of phosphoryl
CC       transfer upon ATP binding. Assembling and dissambling the active center
CC       during each catalytic cycle provides an effective means to prevent ATP
CC       hydrolysis. {ECO:0000250|UniProtKB:P69441}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
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DR   EMBL; X70086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S34407; S34407.
DR   AlphaFoldDB; P35141; -.
DR   SMR; P35141; -.
DR   UniPathway; UPA00588; UER00649.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Kinase; Nucleotide biosynthesis;
KW   Nucleotide-binding; Transferase.
FT   CHAIN           1..>40
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000158850"
FT   REGION          30..>40
FT                   /note="NMP"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         10..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   BINDING         31
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P69441"
FT   NON_TER         40
SQ   SEQUENCE   40 AA;  4254 MW;  E462253D12826B14 CRC64;
     MNIILMGLPG AGKGTQASEI VKKFPIPHIS TGDMFIKAIK