ID A0A316AKI7_9BACT Unreviewed; 583 AA.
AC A0A316AKI7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=D-alanine-D-alanine ligase {ECO:0000313|EMBL:PWJ58283.1};
GN ORFNames=CLV98_104141 {ECO:0000313|EMBL:PWJ58283.1};
OS Dyadobacter jejuensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1082580 {ECO:0000313|EMBL:PWJ58283.1, ECO:0000313|Proteomes:UP000245880};
RN [1] {ECO:0000313|EMBL:PWJ58283.1, ECO:0000313|Proteomes:UP000245880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 100346 {ECO:0000313|EMBL:PWJ58283.1,
RC ECO:0000313|Proteomes:UP000245880};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC {ECO:0000256|ARBA:ARBA00010871}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PWJ58283.1}.
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; QGDT01000004; PWJ58283.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316AKI7; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000245880; 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: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; -; 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 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; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR SUPFAM; SSF52440; PreATP-grasp domain; 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|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:PWJ58283.1};
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:UP000245880}.
FT DOMAIN 221..432
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 583 AA; 65770 MW; B985CE0814DE5132 CRC64;
MRIGIFFGGP SREREISFSG GKTAFEYLDQ SLFEPVPVFV DSFGRFILLN NSLMYRPGIR
SFYPAVDGQN GSFNLYIESF PELAQKPVPA EIGVELLPTD FGKHFDFAFL AMHGPDCEDG
AIQGLLEWYR IPYSGPGLMG SALAIDKILQ NDMIALVNQQ EKKSWTLTHH QWIPQEQEIL
FRVLKKHLGL PLVIKAPHQG SSIGVAIVKN DSLEEFISAV DQCFFQLTLR APEWLGWNQS
QKQNWAQRIA NLDEGIGYPV MANGLELIHH PDTLIAFVEG YFGANPSGEL LLSSSNAEDQ
VLIEEFIEGQ EFSCGCIQFD NGEPLALPPS EVVKMVDVFD FNSKYKPGAS RKRIPVDTTL
EKNQEIQQMI TAVFKQLGMT ACVRIDGFLT ADGRILLHDP NTIPGMSPTS FIFKQMAEIG
LDVTQALTYL VRQSLRERIR LGKNTWEWRK LLKELDVAII ERSTGKKKQI GVLFEDNNDQ
YQLARQRFGA INATGTQEAI PVLQAKDGSV YRLTKPMMFK DTIVDVQDLM ERPRHALLQE
TSQRAQTLTH FFAGTVDFEI YKVKDKDLIG SIDEWVVVSQ DYT
//
