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Database: UniProt
Entry: A0A0K1NGE2_9BURK
LinkDB: A0A0K1NGE2_9BURK
Original site: A0A0K1NGE2_9BURK 
ID   A0A0K1NGE2_9BURK        Unreviewed;       666 AA.
AC   A0A0K1NGE2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=ATP-grasp domain-containing protein {ECO:0000259|PROSITE:PS50975};
GN   ORFNames=ADJ79_02450 {ECO:0000313|EMBL:AKU67953.1};
OS   Ottowia sp. oral taxon 894.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Ottowia.
OX   NCBI_TaxID=1658672 {ECO:0000313|EMBL:AKU67953.1, ECO:0000313|Proteomes:UP000056623};
RN   [1] {ECO:0000313|Proteomes:UP000056623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W10237 {ECO:0000313|Proteomes:UP000056623};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012073; AKU67953.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K1NGE2; -.
DR   STRING; 1658672.ADJ79_02450; -.
DR   KEGG; oto:ADJ79_02450; -.
DR   PATRIC; fig|1658672.3.peg.681; -.
DR   Proteomes; UP000056623; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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   Gene3D; 3.40.1190.10; Mur-like, catalytic domain; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013651; ATP-grasp_RimK-type.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR044019; Cyanophycin_syn_N.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   PANTHER; PTHR21621:SF0; BETA-CITRYLGLUTAMATE SYNTHASE B-RELATED; 1.
DR   PANTHER; PTHR21621; RIBOSOMAL PROTEIN S6 MODIFICATION PROTEIN; 1.
DR   Pfam; PF18921; Cyanophycin_syn; 1.
DR   Pfam; PF08443; RimK; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF53623; MurD-like peptide ligases, catalytic domain; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN          229..307
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   666 AA;  70887 MW;  A7CA301A5F999C7D CRC64;
     MAAPQRKFAD MKILRMNWVR GPGVWTYRSI IEAVLDIGEL EDFPSNTIPG YYERLTAWLP
     GLVEHKCGVG ERGGFLQRLR EGTWPGHVME HVALELQMQA GMNTAFGKTR MTGEHAVYKV
     VIRAFDEAVG RLALESARDL VMAAINGTPY DVPAAIARLK ALGEQRCFSA GTACIVDAAL
     ARGIPCIRLN ESNLVQLGHG AAQRRIWATT TDRTSAIAAG ISRDKDLLRG LLKGAGIPVP
     EGRVANSAED AWEAAEDIGL PVTVKSAIGG RERGLALNLS TREQVMAAWQ AADALGDDVI
     VEKFIPGHAC RLLVAGGRVV AATRYAEAHS TQNGSDATSQ IHPGTAALAA LAVRVTGLDI
     AGVDLVAQDL AAPLPGQGVI VGVHAGPDLR MHLRPSVYNP PPVGEAIVEH LFPLGESGRI
     PIVGMLGGGA SSFAPRLVSS WLHLHGLRTA LACQEGLFLG ARQLSKSDSR GYDAGERMLI
     NRTVQAAVFE TTPRHILAEG LPYDRCQVGV VLAMPSHEGL QEHYVSEAQQ MPGVARTQVD
     VVLPTGAAVL NADDPAVLAL AEYSDGEVLL FSLDEQNPAL TAHRARGGRV VFARPQGVVL
     AQGSGPEQML SVPPSTRTRI GCDAPDDVRR HILAAVAAAW ALNLPIELVH AGLLHMRKSV
     AMSAYH
//
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