ID   A0A378JPG1_9GAMM        Unreviewed;       908 AA.
AC   A0A378JPG1;
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=Glutamine synthetase adenylyltransferase {ECO:0000313|EMBL:STX52173.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:STX52173.1};
GN   Name=glnE {ECO:0000313|EMBL:STX52173.1};
GN   ORFNames=NCTC13316_02277 {ECO:0000313|EMBL:STX52173.1};
OS   Legionella busanensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=190655 {ECO:0000313|EMBL:STX52173.1, ECO:0000313|Proteomes:UP000254794};
RN   [1] {ECO:0000313|EMBL:STX52173.1, ECO:0000313|Proteomes:UP000254794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC13316 {ECO:0000313|EMBL:STX52173.1,
RC   ECO:0000313|Proteomes:UP000254794};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; UGOD01000001; STX52173.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A378JPG1; -.
DR   Proteomes; UP000254794; Unassembled WGS sequence.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 1.20.120.1510; -; 1.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:STX52173.1}; Transferase {ECO:0000313|EMBL:STX52173.1}.
FT   DOMAIN          33..266
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          290..423
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          551..780
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          804..882
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   908 AA;  105480 MW;  A12E1B8A94CF637B CRC64;
     MLTIPKLLQS NYILFDKYFS NLEHPLREVV KTLLAVSNYA GKQIETLNYL LTQDDWQKQL
     NFIDYKNSLQ QLYTETNQPF NKFIRNFRHY HFLRHLLREL SGLATVEETM LSWSDCADAL
     IMFTLNYCKQ EMTNRYGHPK DEAGNLVDLY VLAMGKLGGQ ELNYSSDIDL IMAFSASGYT
     NGEQHVDNQY FFTKVVQLFI QLMQNVTEDG FVFRVDLRLR PNGESGALVS SLAAMETYYQ
     EQGRDWERYA MIKARLISAS PALRAQWFKK LITPFVYRRY IDFSVIESLR SMKAMIEREV
     QLNPTLDDIK RGFGGIREVE FIVQSIQLIR GGRLPRLQQT NLVNALSALK EEKLFSRTDV
     LKQAYLFLRK LENCLQSEND QQIHALPTEP IKQAKIALAM GFASWDSLLK IVQRFRKIIR
     HLFLSVLKQA IDYDNNDKLL DSQLNNVWQG HAESTMAINL LASLGYQDAE RCYQLLSNFR
     HGSRCRRLNQ AARLRLDRFM TLLLRELANV ANTGEVLLNV IHLLENIVTR SAYITLFTEN
     PQALRELFIW FNNSAFIRGL LVNHPFLLEI LLDQGQEWQP ASRKQLQEQL QKKLLESNDI
     ELQEEILRQF KLTNWLLIAR AEQQSTVTAL QSAHFLSLVA EVIVEQVVKL AFIELGKRYP
     QIPELKSHFA IIAYGKLGSQ EMNYNSDLDL VFIYDNQLQE ESLVTRLTQK ILHMLTTRSQ
     SGLLYKVDTR LRPSGEAGLL VSAIKSFIDY QQNQAWLWEH QALIRARVIF GNTTIHSQFK
     NLKQNILLIE RPKEWVFKEI KAMRQKINRH LKGEDEIKYT PGGLIDLEFF VQFLVLTNPI
     QELSRETNTL SLIKKLADCK VIESEVFKIL TSAYKFYHKI LHQNILASSE VINSQDKCKE
     VLSIVNFH
//