ID   F7XUC3_MIDMI            Unreviewed;       575 AA.
AC   F7XUC3;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-Ala-D-Ala ligase {ECO:0000256|HAMAP-Rule:MF_00047};
DE   AltName: Full=D-alanylalanine synthetase {ECO:0000256|HAMAP-Rule:MF_00047};
GN   Name=ddlA {ECO:0000313|EMBL:AEI89482.1};
GN   Synonyms=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   OrderedLocusNames=midi_01206 {ECO:0000313|EMBL:AEI89482.1};
OS   Midichloria mitochondrii (strain IricVA).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Candidatus Midichloriaceae; Midichloria.
OX   NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI89482.1, ECO:0000313|Proteomes:UP000006639};
RN   [1] {ECO:0000313|EMBL:AEI89482.1, ECO:0000313|Proteomes:UP000006639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IricVA {ECO:0000313|EMBL:AEI89482.1,
RC   ECO:0000313|Proteomes:UP000006639};
RX   PubMed=21690562; DOI=10.1093/molbev/msr159;
RA   Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
RA   Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
RA   Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
RT   "Phylogenomic evidence for the presence of a flagellum and cbb3 oxidase in
RT   the free-living mitochondrial ancestor.";
RL   Mol. Biol. Evol. 28:3285-3296(2011).
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + 2 D-alanine = ADP + D-alanyl-D-alanine + H(+) +
CC         phosphate; Xref=Rhea:RHEA:11224, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57822, ChEBI:CHEBI:456216; EC=6.3.2.4;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00047};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871, ECO:0000256|HAMAP-Rule:MF_00047}.
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DR   EMBL; CP002130; AEI89482.1; -; Genomic_DNA.
DR   AlphaFoldDB; F7XUC3; -.
DR   STRING; 696127.midi_01206; -.
DR   KEGG; mmn:midi_01206; -.
DR   HOGENOM; CLU_473941_0_0_5; -.
DR   OrthoDB; 9813261at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000006639; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR005548; Cell_div_FtsQ/DivIB_C.
DR   InterPro; IPR005905; D_ala_D_ala.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR034746; POTRA.
DR   InterPro; IPR013685; POTRA_FtsQ_type.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   NCBIfam; TIGR01205; D_ala_D_alaTIGR; 1.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF03799; FtsQ_DivIB_C; 1.
DR   Pfam; PF08478; POTRA_1; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS51779; POTRA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW   ECO:0000256|HAMAP-Rule:MF_00047};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000313|EMBL:AEI89482.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006639};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        343..361
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          101..301
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          380..448
FT                   /note="POTRA"
FT                   /evidence="ECO:0000259|PROSITE:PS51779"
SQ   SEQUENCE   575 AA;  64744 MW;  8635E4385156424D CRC64;
     MNKHIVLLVG GVSREREVSQ ISGESVRNAL LSLGYRVTVV DPSENLASEL IKLRPDIVFN
     CLHGTFGEGG SIPGLLELLR IPYTHSGVTA SAIAMDKILT KKMAQTCDIN TPKYVKIEKS
     ALFTMLEKGE DPMPKPYVIK AVQQGSSIGI YLVIDENSDK PKKAEWTFGE QILVEEYIPG
     QELSVAVLND KALGVLELRP KTNFYDYTAK YSDGVTEHVH PAEIPQEVYL EAMKRAEEMH
     KALGCRTVSR SDFRYNNIGS ADGLFFLEIN THPGFTNLSI VPDIASRRGI SFEQIIEQLL
     KDAKMRNNAV KIAKYTYLDT DVHYGKQISS LLQPAREKPF KKIIRVYILF LLGVAAIFYI
     LTKLCTNEVD QFVDKLINKT VISELNICGN IQVSKEEIIN TLDLSLPLEV SYINASHIKE
     ELLKNPLIKD VEVKINLPNI LSLLVTERQP FALWFDQKQF HLIDEEGFIV KACVEFQEKE
     NKYIIAAGTD SNNQLQNLLD ELKGYSISKK LFAVQLISNR RWNILLKNGL IVKLPENNVK
     EALVALDLVL ENYSPSKPFN IIDLRLAPGK VYAVF
//