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Database: UniProt
Entry: F4LNJ1_TREBD
LinkDB: F4LNJ1_TREBD
Original site: F4LNJ1_TREBD 
ID   F4LNJ1_TREBD            Unreviewed;       695 AA.
AC   F4LNJ1;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Glutamine synthetase catalytic region {ECO:0000313|EMBL:AEE15845.1};
GN   OrderedLocusNames=Trebr_0398 {ECO:0000313|EMBL:AEE15845.1};
OS   Treponema brennaborense (strain DSM 12168 / CIP 105900 / DD5/3).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC   Treponema.
OX   NCBI_TaxID=906968 {ECO:0000313|EMBL:AEE15845.1, ECO:0000313|Proteomes:UP000006546};
RN   [1] {ECO:0000313|Proteomes:UP000006546}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12168 / CIP 105900 / DD5/3
RC   {ECO:0000313|Proteomes:UP000006546};
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Pagani I.,
RA   Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Gronow S.,
RA   Wellnitz S., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Treponema brennaborense DSM 12168.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC       {ECO:0000256|PROSITE-ProRule:PRU01330, ECO:0000256|RuleBase:RU000384}.
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DR   EMBL; CP002696; AEE15845.1; -; Genomic_DNA.
DR   RefSeq; WP_013757564.1; NC_015500.1.
DR   AlphaFoldDB; F4LNJ1; -.
DR   STRING; 906968.Trebr_0398; -.
DR   KEGG; tbe:Trebr_0398; -.
DR   eggNOG; COG3968; Bacteria.
DR   HOGENOM; CLU_024307_0_0_12; -.
DR   OrthoDB; 9807095at2; -.
DR   Proteomes; UP000006546; Chromosome.
DR   GO; GO:0004356; F:glutamine synthetase activity; IEA:InterPro.
DR   GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.20.120.1560; -; 1.
DR   Gene3D; 3.30.590.10; Glutamine synthetase/guanido kinase, catalytic domain; 1.
DR   InterPro; IPR040577; Gln-synt_C.
DR   InterPro; IPR008147; Gln_synt_N.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR008146; Gln_synth_cat_dom.
DR   InterPro; IPR027303; Gln_synth_gly_rich_site.
DR   InterPro; IPR022147; GSIII_N.
DR   PANTHER; PTHR42974; GLUTAMINE SYNTHETASE; 1.
DR   PANTHER; PTHR42974:SF1; TYPE-3 GLUTAMINE SYNTHETASE; 1.
DR   Pfam; PF00120; Gln-synt_C; 1.
DR   Pfam; PF18318; Gln-synt_C-ter; 1.
DR   Pfam; PF12437; GSIII_N; 1.
DR   SMART; SM01230; Gln-synt_C; 1.
DR   SUPFAM; SSF55931; Glutamine synthetase/guanido kinase; 1.
DR   PROSITE; PS00181; GLNA_ATP; 1.
DR   PROSITE; PS51986; GS_BETA_GRASP; 1.
DR   PROSITE; PS51987; GS_CATALYTIC; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006546}.
FT   DOMAIN          62..151
FT                   /note="GS beta-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS51986"
FT   DOMAIN          156..585
FT                   /note="GS catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS51987"
SQ   SEQUENCE   695 AA;  77069 MW;  9D5ECD0859865B6F CRC64;
     MSTVPELFGS MVFNETVMKE RLPKDTFKVL KKTMDEGSPL EEGVANIVAN AMKDWAVEKG
     ATHYTHWFQP MTGITAEKHD SFISPQTDGT VIMEFSGKEL IKGEPDGSSF PSGGIRATCE
     ARGYTAWDPT SPAFIKDGSL CIPTAFCSYG GEALDKKTPL LRSMDAIDKQ AKRILKLFGK
     TVKRVCTTVG PEQEYFLIDK TLWEQRKDLI YTGRTLFGAK PPKGQELEDH YFGTIKPRIS
     AYMKELDEEL WKLGILAKTK HNEVAPAQHE MAPIFTTTNI AADDNQLTME MMKKVAARHG
     LVCLLHEKPF AGVNGSGKHN NWSLSTDKGE NLLEPGSTPE ENAQFLLILT AIIKGIDEYQ
     DLLRASVATA GNDHRLGANE APPAIISMFL GDELDSILES IRTGKPYDRK AKEVLRLGVD
     ALPAFPKDNT DRNRTSPFAF TGNKFEFRSL GSSLSISCPN IMLNTIVAEE FAQFADILEK
     SKDFTKDLNE LIKKTLSKHH RIIFNGNGYS DEWVREAEKR GLLNLKTTSD AMPYFIAQKN
     IDMFKKHGVY TGTEMKARYE IQMEEYVKVL NIEALTMIEM TRKQIVPAVF KYLQSVSATA
     AGIKALVPGA ECSAEAGIVQ TVSGLCDAAV KKIAALETAM LNSKECADIT AEAKFYTASV
     IPAMTELRAV ADELETLVGE DYWPFPTYGD LLFRV
//
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