ID   A0A126P7M8_9BACT        Unreviewed;       910 AA.
AC   A0A126P7M8;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:AMJ65130.1};
GN   ORFNames=AXW84_06600 {ECO:0000313|EMBL:AMJ65130.1};
OS   Hymenobacter sp. PAMC 26628.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ65130.1, ECO:0000313|Proteomes:UP000059956};
RN   [1] {ECO:0000313|EMBL:AMJ65130.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ65130.1};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CP014304; AMJ65130.1; -; Genomic_DNA.
DR   RefSeq; WP_068230338.1; NZ_CP014304.1.
DR   AlphaFoldDB; A0A126P7M8; -.
DR   STRING; 1484118.AXW84_06600; -.
DR   KEGG; hyz:AXW84_06600; -.
DR   OrthoDB; 9813261at2; -.
DR   Proteomes; UP000059956; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 3.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
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; 4.
DR   Pfam; PF01820; Dala_Dala_lig_N; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 3.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 3.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AMJ65130.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059956}.
FT   DOMAIN          157..216
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          228..445
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          646..895
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   910 AA;  98777 MW;  9F29C27B54B30D24 CRC64;
     MRIGIFFGGT SREREISFAG GRTVFDNLDK ALFQPVPIFV DSLGRFLLLD WQYLYKGTIR
     DFYPPVAALP PTAHPWSVYV ESLGLPTGPL LDPDLSRVGR QVMPEELPLL MDFAFLALHG
     PGGEDGAIQG LLEWLGVPYS GSGILPSAFG IDKVAQKKLL QATGLATPKF RVITAAAWDA
     ADPAAVLADT VGGLGLPLVF KAPHQGSSIG ISMLKESNLA AFEAAMERSL FRKKLTRAEW
     QGLGEEGQRA WVQHLADIRE GIGLPVVLEA AAGAPATDAL EPIYHPEALL GALSAWFETA
     DAVRLASTHG ETAVLVEAFV AGREFSCIVV ENERGEPLAL PPTEILKGEE LFDYRSKYLP
     GLARKITPID LPEAEIERIR QQCQAMFRTF GFQVYARLDG FIQADGTIFL NDPNTTSGML
     PASFFFHQAA EIGLNPSQFL TYLIRMSLAA RRAGGMAPFK LGALLATLDA AVADRQQAGA
     GGRIRVAVIM GGYSSERHIS VESGRNIFEK LSSSAKYAPV PVFLTGSAQE HRLYVLPINV
     MLKDNADDIR EKIEHAEAGE GPHPILAKIQ AEAGALTRTY AGQGLVQPRR ISFAELAELA
     DEVFIALHGR PGEDGALQQE LERFGLPYNG SGVASSAVTI NKFETNRRLR AAGLLVADHR
     MAPRLEWAAD PESFYRSLET QFPYPFIAKP ADDGCSSAVK KIKNRAELVA FTELMFRDQE
     DLLAGPAEVL HLGFKEEFPQ KDAFLVETLI SRDGAAHFLE VTGGLLTSYD EDGRLAIEVF
     EASEALANGE VLSLEEKFLA GEGQNITPAR YAAEPGERQR VSNEVKAVLH RVAEVLDIQG
     YARIDAFVRV RQSGAVEVII IEVNSLPGMT PATCIFHQTA LAGYTPYQFV DRILEFGKAR
     AGRVAAGAPA
//