ID   A0A346NKC5_9ALTE        Unreviewed;       493 AA.
AC   A0A346NKC5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=Carboxylate--amine ligase {ECO:0000313|EMBL:AXR05982.1};
GN   ORFNames=D0Y50_06055 {ECO:0000313|EMBL:AXR05982.1};
OS   Salinimonas sediminis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Alteromonas/Salinimonas group; Salinimonas.
OX   NCBI_TaxID=2303538 {ECO:0000313|EMBL:AXR05982.1, ECO:0000313|Proteomes:UP000262073};
RN   [1] {ECO:0000313|EMBL:AXR05982.1, ECO:0000313|Proteomes:UP000262073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N102 {ECO:0000313|EMBL:AXR05982.1,
RC   ECO:0000313|Proteomes:UP000262073};
RA   Cao J.;
RT   "Salinimonas sediminis sp. nov., a piezophilic bacterium isolated from a
RT   deep-sea sediment sample from the New Britain Trench.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP031769; AXR05982.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A346NKC5; -.
DR   KEGG; salm:D0Y50_06055; -.
DR   OrthoDB; 9800957at2; -.
DR   Proteomes; UP000262073; 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: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; IPR025839; RLAN_dom.
DR   PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 1.
DR   Pfam; PF14401; RLAN; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Ligase {ECO:0000313|EMBL:AXR05982.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          293..485
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   493 AA;  54998 MW;  9E08435F127F13F3 CRC64;
     MHNTLIVADD LSPFAQTSLN VITFDSYLAD FPKLNEPKTR VINLCDTGKY LSQGYYCSLL
     AQARKHGVLP AVKTINDLRM TDEGHGLPRL SLPDTFIWPD NESLPDAIYV LFGQTKDQHF
     AKVAEVAFRY YPCPILKLTV HLAGENAVTS TGGPIGVVEC EAIGFNDVPA SLQGFAIERL
     QAFTESHWRE RPQSKKMRWD MAILVNPDET TPPSDKKAIS QFVKAAHNVG INAEVVSHLR
     PDDVGHYDAL LIRETTAIDH HTYRLARAAE REGLVVIDDT QSILRCCNKV FLQDAFTYQQ
     VPAPQSQFVS SHEDSVCEKL ISDLGLPLVL KLPESSFSRG VYKVEDAAEL KARLVEMLSA
     SALVLVQEYV YTEFDWRIGM LGGKPIYACK YYMARNHWQI YNHKGDGTDS GDFATMPTFE
     VPKAVLQAAT KAAKVVGNGL YGVDIKQSGN KVYVIEVNDN PSIDSGVEDK YLGKALYELI
     MQEFVNRLEL RGR
//