ID A0A2T1G075_9CYAN Unreviewed; 391 AA.
AC A0A2T1G075;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-alanyl-alanine synthetase {ECO:0000313|EMBL:PSB50644.1};
GN ORFNames=C7B67_13760 {ECO:0000313|EMBL:PSB50644.1};
OS filamentous cyanobacterium Phorm 6.
OC Bacteria; Cyanobacteriota.
OX NCBI_TaxID=2107706 {ECO:0000313|EMBL:PSB50644.1, ECO:0000313|Proteomes:UP000239157};
RN [1] {ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|Proteomes:UP000239157};
RA Moore K., Momper L.;
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PSB50644.1, ECO:0000313|Proteomes:UP000239157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Phorm 6 {ECO:0000313|EMBL:PSB50644.1,
RC ECO:0000313|Proteomes:UP000239157};
RA Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT "The ancient ancestry and fast evolution of plastids.";
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:PSB50644.1}.
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; PVWI01000100; PSB50644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T1G075; -.
DR OrthoDB; 9813261at2; -.
DR Proteomes; UP000239157; Unassembled WGS sequence.
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 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; IPR011095; Dala_Dala_lig_C.
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; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW Reference proteome {ECO:0000313|Proteomes:UP000239157}.
FT DOMAIN 143..369
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 391 AA; 44085 MW; 1DDB88EEC99BA9B0 CRC64;
MTATSISMNH LDYDFNLLPE YLELLFAKLR IAVVFGGDCD RAGSVIYKTH NPRSWKSYKI
VAREISQALV EIGFKHVFVI PDDMNLPEQL KQKNIHLVWL NTGGVQGYNP VCHTPALLEM
LGMPYIGHNP LNSSTLDNKH AFKRELQSLG IQTAPFMTWH PSQGILLPNL HDRFALTFGE
YQGPFVVKPV SGRASLHVYF VDKIEGLSQA VSEVHRATHN TALIEKYLPG QEFCVAVCGY
VTYANGAFSK NTKPFAFSTI ERVLESEEHI FTSMDKKAIT TDRGRLMGPE EPELKQELIE
LARKIYWEFS LNSLVRIDVR SDADGSLFVL EANPKPDLKH PEENVTSLVA LGLAEYGMSY
NDLILSLLAD RLDYLLTQHI EIIPHIVDLL C
//
