ID   SYG_CHLTR               Reviewed;        1003 AA.
AC   P0CE22; O84802; Q46371;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   02-MAR-2010, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Glycine--tRNA ligase;
DE   AltName: Full=Glycyl-tRNA synthetase;
DE            Short=GlyRS;
DE            EC=6.1.1.14;
DE   Includes:
DE     RecName: Full=Glycine--tRNA ligase alpha subunit;
DE     AltName: Full=Glycyl-tRNA synthetase alpha subunit;
DE   Includes:
DE     RecName: Full=Glycine--tRNA ligase beta subunit;
DE     AltName: Full=Glycyl-tRNA synthetase beta subunit;
GN   Name=glyQS; Synonyms=glyQ, glyS; OrderedLocusNames=CT_796;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; AE001273; AAC68391.1; -; Genomic_DNA.
DR   PIR; B71469; B71469.
DR   RefSeq; NP_220316.1; NC_000117.1.
DR   RefSeq; WP_010725349.1; NC_000117.1.
DR   AlphaFoldDB; P0CE22; -.
DR   SMR; P0CE22; -.
DR   STRING; 813.O172_04430; -.
DR   EnsemblBacteria; AAC68391; AAC68391; CT_796.
DR   GeneID; 884595; -.
DR   KEGG; ctr:CT_796; -.
DR   PATRIC; fig|272561.5.peg.875; -.
DR   HOGENOM; CLU_007220_1_1_0; -.
DR   InParanoid; P0CE22; -.
DR   OMA; LPIPKRM; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00733; GlyRS_alpha_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00254; Gly_tRNA_synth_alpha; 1.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR002310; Gly-tRNA_ligase_asu.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF02091; tRNA-synt_2e; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01044; TRNASYNTHGA.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00388; glyQ; 1.
DR   TIGRFAMs; TIGR00211; glyS; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 2.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..1003
FT                   /note="Glycine--tRNA ligase"
FT                   /id="PRO_0000072890"
FT   REGION          1..310
FT                   /note="Glycine--tRNA ligase alpha subunit"
FT   REGION          311..1003
FT                   /note="Glycine--tRNA ligase beta subunit"
SQ   SEQUENCE   1003 AA;  112577 MW;  79EB918FE19D39E9 CRC64;
     MSSQPLTLQT MMAAILNFWS EQGCIIHQGY DLEVGAGTFN PATFLQSLGP EPFRTAYIEP
     SRRPQDGRYG QHPNRLQKYH QLQVILKPVP ENFLSLYLES LKVIGLNLVD HDIRFVHDDW
     ENPTIGAWGL GWEVWLNGME ITQLTYFQAV GSKPLDAISG EITYGVERIA MYLQKKNSVY
     DVMWNDSLTY GDITQYAEQA WSQYNFETAN TTMWLKHFDD FSAEALATLD QGLPLPAYDF
     VIKASHAFNM LDSRGVISVT ERTRYIAKIR QLARAAADKY VAWRESLGFP LLKTPPSTPT
     VTPKKIPTIC QPEDFLLEIG SEELPATFVP TGIQQLESLA KKLLADHGIA YKHLEVLGTP
     RRLALCIEGL SHVTIRPESE KKGPPLSLLF MTDGSVSPQG EQFFSSHGLS ISHRSALDQP
     SAIWRVRSIN GTDYLFLVIP EERKETAAIL VNELPQLIRS IRFPQKMTWD NGGVEYARPI
     RWLVALYGDQ ILPISLGFVS SGNTSWGHRQ LDNRQLTIPS SNMYVDTLRS ACVIVSQKER
     RAIIKQGLQN LTGDQIVAIA PEHLIDETVF LTEHPFVISA QFDPAFCSLP KELLIAEMIQ
     HQRYFPTQNM QGEITNRFLI VCDNSPTDSI VEGNEKALAP RLTDGNFLFK QDLLTPLSSF
     VEKLKSVTYF ESLGSLADKT SRLKLHLEEA YALLPLCAKE DIDTAIHYCK ADLVSSVVNE
     FPELQGIMGR YYLQNASLSR AAALAIGEHL QHITLGSSIS TTGALLSILD RIDNLLSCFI
     LGLLPTSSHD PYALRRQSLE ILTLLYTTQS SVDIEDLFAR LIRHFPSSIP NTVWSPEAVL
     SKLNTFVWGR LRTILSSLGF DKEVIATVLT DNCPKNPLTI IQSAQSIQEL KNTQILKTIA
     AMYNRLKKIL ASLSFSVTEQ MFSLQSAEDL LFKQALDRFV EETTALPISS KDYLHLLKEL
     AQSTELFLDS VRVASDDEST RNQRIALLIA AQKCFGFYAW GVL