ID   A0A5M9Z1J7_9LACO        Unreviewed;       399 AA.
AC   A0A5M9Z1J7;
DT   26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT   26-FEB-2020, sequence version 1.
DT   27-NOV-2024, entry version 17.
DE   RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020};
DE            EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020};
DE   AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020};
GN   Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020};
GN   ORFNames=F1C09_07705 {ECO:0000313|EMBL:KAA8812113.1};
OS   Lactobacillus crispatus.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=47770 {ECO:0000313|EMBL:KAA8812113.1, ECO:0000313|Proteomes:UP000324504};
RN   [1] {ECO:0000313|EMBL:KAA8812113.1, ECO:0000313|Proteomes:UP000324504}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCK2488 {ECO:0000313|EMBL:KAA8812113.1,
RC   ECO:0000313|Proteomes:UP000324504};
RA   Pan M., Hidalgo-Cantabrana C., Barrangou R.;
RT   "Comparative analysis of L. crispatus genomes revealed niche specific
RT   adaptation to different host and body sites.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC       ATP. Can also catalyze the reverse reaction. {ECO:0000256|HAMAP-
CC       Rule:MF_00020}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC         ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00020};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
CC       Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP-Rule:MF_00020};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC       acetyl-CoA from acetate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020}.
CC   -!- SIMILARITY: Belongs to the acetokinase family.
CC       {ECO:0000256|ARBA:ARBA00008748, ECO:0000256|HAMAP-Rule:MF_00020,
CC       ECO:0000256|RuleBase:RU003835}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAA8812113.1}.
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DR   EMBL; VUAV01000048; KAA8812113.1; -; Genomic_DNA.
DR   RefSeq; WP_057726928.1; NZ_VUAV01000048.1.
DR   AlphaFoldDB; A0A5M9Z1J7; -.
DR   UniPathway; UPA00340; UER00458.
DR   Proteomes; UP000324504; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006083; P:acetate metabolic process; IEA:TreeGrafter.
DR   GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_00020; Acetate_kinase; 1.
DR   InterPro; IPR004372; Ac/propionate_kinase.
DR   InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR   InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR   InterPro; IPR043129; ATPase_NBD.
DR   NCBIfam; TIGR00016; ackA; 1.
DR   PANTHER; PTHR21060; ACETATE KINASE; 1.
DR   PANTHER; PTHR21060:SF15; PROPIONATE KINASE PDUW; 1.
DR   Pfam; PF00871; Acetate_kinase; 1.
DR   PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR   PRINTS; PR00471; ACETATEKNASE.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS01075; ACETATE_KINASE_1; 1.
DR   PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00020};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00020};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00020};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00020};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00020};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00020}.
FT   ACT_SITE        146
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         206..210
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         281..283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         333..337
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   BINDING         384
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   SITE            178
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT   SITE            239
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ   SEQUENCE   399 AA;  44049 MW;  2B467FEDBF680959 CRC64;
     MKKILAINSG SSSFKFKLFT FPDEKVISEG MADRVGLNGS TFTIKVKGEK HQEKVDIPDS
     ETAVTILLEN LKKYDLIDDP KEIIGIGHRI VAGGEEFKDS TLIDEKSLQK IYDLKQYAPL
     HNTAEADVIK AFMKVLPGVP EVAVFDTSFH QTLDPVHYLY SLPYKYYEKY GARKYGAHGT
     SVRYVSQKAA EIMKRDLKDL KLIVCHLGSG ASVTAVKDGK SFDTSMGFSP MAGITMSSRS
     GDVDPSLLAF VMKKENLDAD QMLKVLNNES GLLGISGISP DMRDLRGDMT KLEGEKKKRA
     DLARNIFINR IIRYVGAYTL EMRGLDGIAF TAGVGEHDFG VREHVMDSLE LLGLKPDSAA
     NKENATIITK PNSTIVGMVI PTNEELMIER DVVRVAGLK
//