ID M8C8Q2_AEGTA Unreviewed; 901 AA.
AC M8C8Q2;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EnsemblPlants:EMT30463};
OS Aegilops tauschii (Tausch's goatgrass) (Aegilops squarrosa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Pooideae; Triticodae; Triticeae; Triticinae; Aegilops.
OX NCBI_TaxID=37682 {ECO:0000313|EnsemblPlants:EMT30463};
RN [1] {ECO:0000313|EnsemblPlants:EMT30463}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
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DR AlphaFoldDB; M8C8Q2; -.
DR EnsemblPlants; EMT30463; EMT30463; F775_28159.
DR ExpressionAtlas; M8C8Q2; baseline.
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: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; 2.
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; 2.
DR Pfam; PF01820; Dala_Dala_lig_N; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR PROSITE; PS50975; ATP_GRASP; 2.
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};
KW 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984}.
FT DOMAIN 137..378
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 797..859
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 901 AA; 99589 MW; 3C275BCDEEFCB57E CRC64;
MSGHRPSNAI SPKYLTCPSL VQMERGRQSI CMDLNFALRL FLQSLCLASL SPPTNLGEDL
LVSCYYIDCG MNAFAISPAQ LYSNTPSDFD FKLESLAQEF STLSEFAEHL AANVDIVFPV
IHGKFGEDGG IQELLEKANV PFVGTPSNEC LRAFDKHNAS LELDAQGFLT VPNFLVEVKP
TRAGSSIGVV VAYGANEAAE KAEGIFSEGI DNKVIIEVFL EGGCEFTAIV LDVGTANNSE
PIVLLPTEVE LQSSISSDIQ EDTIFNYRRK YLPTQQVAYH TPPRFPAEVI DCIRKGVSLL
FRHFGLRDFA RIDGWFLPSP ATSLPSSENG VKFGNTEYGA VLFTDINLIS GMEQTSFLFQ
QASKVGFSHS RILRTIVQHA CSRFPSLVTS NNAWTALSRK MQSAKQALII PNGTCKQKAF
VIFGGDTSER QVSLMSGTNV WLNLQGFDDL DVTPCLLAPS NGYSSHNEDF SESSRDVWTL
PYSLVLRHTT EEVHAACFEA IEPERVEITS RLRNQVMKEL ERALSKQDWF AGFDITDEQP
IKYSLQQWID YVKEAKAVVF IAVHGGIGED GTIQSLLESA GVPYTGPGPI ASRTCMDKVA
TSLAVDHLAS YGIHTIPKDV RAREELLKSS LVDIWNDLKA KLQTETLIKK LSVIRCPEDL
EVYANALRGT LPRLPANCLS KAHGVIEMPV PPPESLIFEP FIETDEIIIS NKSWNDSTRH
LVWKGENEWL EVTVGVVGKR GEMHSLNPSI TVKESGDILS LEEKFQGGTG INLTPPPATI
MSEDALQKCK SCIEMTANTL GLEGFSRIDA FVNVHSGEVL LIEVNTVPGM TPSTVLIHQT
NFLKIISLKL VEAGHFLIQK RLYMIDVSKG NAKRLKMFPI QFMFPSRIIE MFTICADRYI
A
//
