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Database: UniProt/TrEMBL
Entry: A0A0P0F632_AZOBR
LinkDB: A0A0P0F632_AZOBR
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ID   A0A0P0F632_AZOBR        Unreviewed;       316 AA.
AC   A0A0P0F632;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   25-OCT-2017, entry version 17.
DE   RecName: Full=D-alanine--D-alanine ligase {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
DE            EC=6.3.2.4 {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910572};
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=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN   ORFNames=AMK58_03905 {ECO:0000313|EMBL:ALJ34634.1};
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192 {ECO:0000313|EMBL:ALJ34634.1, ECO:0000313|Proteomes:UP000065707};
RN   [1] {ECO:0000313|EMBL:ALJ34634.1, ECO:0000313|Proteomes:UP000065707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sp 7 {ECO:0000313|EMBL:ALJ34634.1,
RC   ECO:0000313|Proteomes:UP000065707};
RA   Millard Andrew;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Cell wall formation. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910576}.
CC   -!- CATALYTIC ACTIVITY: ATP + 2 D-alanine = ADP + phosphate + D-
CC       alanyl-D-alanine. {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00910566}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR039102-3};
CC       Note=Binds 2 magnesium or manganese ions per subunit.
CC       {ECO:0000256|PIRSR:PIRSR039102-3};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00910564};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910582}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
CC       ECO:0000256|SAAS:SAAS00644680}.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00047, ECO:0000256|SAAS:SAAS00910642}.
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DR   EMBL; CP012914; ALJ34634.1; -; Genomic_DNA.
DR   RefSeq; WP_035675402.1; NZ_JPIS01000018.1.
DR   EnsemblBacteria; ALJ34634; ALJ34634; AMK58_03905.
DR   KEGG; abf:AMK58_03905; -.
DR   KO; K01921; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000065707; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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: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; 3.30.1490.20; -; 1.
DR   HAMAP; MF_00047; Dala_Dala_lig; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR005905; D_ala_D_ala.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF01820; Dala_Dala_lig_N; 1.
DR   PIRSF; PIRSF039102; Ddl/VanB; 2.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01205; D_ala_D_alaTIGR; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644673};
KW   Cell shape {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644718};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644792};
KW   Complete proteome {ECO:0000313|Proteomes:UP000065707};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00910562};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644741, ECO:0000313|EMBL:ALJ34634.1};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910568};
KW   Manganese {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910578};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR039102-3,
KW   ECO:0000256|SAAS:SAAS00910590};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000256|SAAS:SAAS00644705};
KW   Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_00047,
KW   ECO:0000256|SAAS:SAAS00644714}.
FT   DOMAIN      108    309       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   METAL       259    259       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       276    276       Magnesium or manganese 1.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       276    276       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
FT   METAL       278    278       Magnesium or manganese 2.
FT                                {ECO:0000256|PIRSR:PIRSR039102-3}.
SQ   SEQUENCE   316 AA;  33675 MW;  51A9825283B8C792 CRC64;
     MTTPHKKHVA VLMGGWSAER EVSLVSGAGV AKALEEEGYR VTAVDVQRDL EGLLRALTDP
     RPDAVFNALH GRGGEDGTIQ GVLEFLGIPY THSGVRAAAV AMDKAMTKAL LAPVGVRSPK
     GLVLTKGELT GGAHPMPAPY IVKPVDEGST VGVTLVREGQ NSPVGDAWTF GERALVEEFI
     PGRELTVGVM GGLDGECRPL TVTEIRFEAQ VYDYTAKYSA GHAVHTVPAQ IPEHVAEEAK
     RLAVLAHRTL GCRGVSRSDF RWDDRKSGTD GLFFLEINNQ PGMTPLSLVP EQAASVGLTY
     GALVAWMVEN AACQLD
//
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