ID A0A1I2QS16_9BACT Unreviewed; 900 AA.
AC A0A1I2QS16;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=ddl {ECO:0000256|HAMAP-Rule:MF_00047};
GN ORFNames=SAMN05421739_10270 {ECO:0000313|EMBL:SFG30059.1};
OS Pontibacter chinhatensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Pontibacter.
OX NCBI_TaxID=1436961 {ECO:0000313|EMBL:SFG30059.1, ECO:0000313|Proteomes:UP000198724};
RN [1] {ECO:0000313|EMBL:SFG30059.1, ECO:0000313|Proteomes:UP000198724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LP51 {ECO:0000313|EMBL:SFG30059.1,
RC ECO:0000313|Proteomes:UP000198724};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOOT01000002; SFG30059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2QS16; -.
DR STRING; 1436961.SAMN05421739_10270; -.
DR OrthoDB; 9813261at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000198724; Unassembled WGS sequence.
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:InterPro.
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; -; 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 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_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; 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, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960, ECO:0000256|HAMAP-
KW Rule:MF_00047};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316,
KW ECO:0000256|HAMAP-Rule:MF_00047};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00047};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00047};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984, ECO:0000256|HAMAP-
KW Rule:MF_00047}.
FT DOMAIN 157..439
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 639..888
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 900 AA; 102206 MW; B25D9A16C424CC84 CRC64;
MKVGIIFGGP SREREISFAG GRTVYDNLDK SLFETVPVFV DSLGNFILLD WQFIYKGTIR
DFYPPVEALP ESEHGLQIYL ESLGELSIEE QDRIIAKAGK RLQPNEFKDH FDFAFLTLHG
PYGEDGSIQG LLEWYHIPYS GSGILPSAIG IDKIAQKEML KQHGFPTPDY RIIKYADWSK
KQNRRQIFEE VKSALHLPLV LKAPHQGSSI GVSIIKEDNF DAFEKSVERS FFTKTIYKSQ
WLALGEEKQL MSMKQLVDIR EGIGMPVVLE DGQIIYHPEE LFNHINHTFH TTATDSITLT
NIEHEQQILV EAFIQGKEFS CIVVQDEQGE PIALPPTEIV KGSEVFDYRS KYLPGLSRKI
TPINLPTEQI QSIRRATSKL FKDFGFNVYA RLDGFITEEG NIFLNDPNTT SGMLPSSFFF
HQAAEIGLNP SQFLTYIIRT SLAERLKTGK DTVRLSRLLQ QLDKSIKDEQ AHRQEKIRVG
VIMGGYSSER HISVESGRNI YEKLSSSVKY EPLPIFLTGS NEAHRLYSIP INIMLKDNAD
DIKEKVLYFE QGGKPHPVLA QIIEEASSIT KKYTGRSLQE PQRITYEQLK NLVDVVFIAL
HGRPGEDGAL QQELEKLYIP YNGSGIRSSQ ITINKYETNE ILGRHGVPVA KHAMAWKEDW
LQDKEAFYQS IEAQFPYPFI AKPADDGCSS AVKKIKNRQE LEAFTTLIFR EMEELDTECA
RTLSLGFKEE FPNKVGFLVE TLISRNGAKH FLEITGGLLT KYNPDGTVSY EVFEASEALA
EGEVLSLEEK FLAGEGQNIT PARYAADPER RQKISDKVKE DLRRVAQILN IEGYARIDAF
VRVLENDEVE TIIIEVNSLP GMTPATCIFH QTAINGYKPY DFIDRILQYG MERTKMKAEI
//
