GenomeNet

Database: UniProt
Entry: K9EBL5_9LACT
LinkDB: K9EBL5_9LACT
Original site: K9EBL5_9LACT 
ID   K9EBL5_9LACT            Unreviewed;       685 AA.
AC   K9EBL5;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   RecName: Full=Glycine--tRNA ligase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            EC=6.1.1.14 {ECO:0000256|HAMAP-Rule:MF_00255};
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit {ECO:0000256|HAMAP-Rule:MF_00255};
DE            Short=GlyRS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   Name=glyS {ECO:0000256|HAMAP-Rule:MF_00255};
GN   ORFNames=HMPREF9698_00375 {ECO:0000313|EMBL:EKU94063.1};
OS   Alloiococcus otitis ATCC 51267.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Alloiococcus.
OX   NCBI_TaxID=883081 {ECO:0000313|EMBL:EKU94063.1, ECO:0000313|Proteomes:UP000009875};
RN   [1] {ECO:0000313|EMBL:EKU94063.1, ECO:0000313|Proteomes:UP000009875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51267 {ECO:0000313|EMBL:EKU94063.1,
RC   ECO:0000313|Proteomes:UP000009875};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Alloiococcus otitis ATCC 51267.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|ARBA:ARBA00000201,
CC         ECO:0000256|HAMAP-Rule:MF_00255};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC       {ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00008226, ECO:0000256|HAMAP-Rule:MF_00255}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKU94063.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGXA01000005; EKU94063.1; -; Genomic_DNA.
DR   RefSeq; WP_003776784.1; NZ_JH992957.1.
DR   AlphaFoldDB; K9EBL5; -.
DR   STRING; 883081.HMPREF9698_00375; -.
DR   PATRIC; fig|883081.3.peg.377; -.
DR   eggNOG; COG0751; Bacteria.
DR   HOGENOM; CLU_007220_2_2_9; -.
DR   Proteomes; UP000009875; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   NCBIfam; TIGR00211; glyS; 1.
DR   PANTHER; PTHR30075:SF2; GLYCINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR   PANTHER; PTHR30075; GLYCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00255};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00255};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00255};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00255};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00255}; Reference proteome {ECO:0000313|Proteomes:UP000009875}.
SQ   SEQUENCE   685 AA;  77541 MW;  43F7B8C2CFE768D5 CRC64;
     MSHQFLYEIG LEELPARFIT DLEAQLKNLV SQFLNDQGLA YSKIKSYSTP RRLAVQVWDL
     ADSQEDKTES FRGPAKKIAL DQDGQWTKAA LGFAKGQGMS ADDIVFKEDK GQDYAFIEKF
     RPGQKADQVL EDISQVVSGL TAPVSMKWGD NHFRFVRPVH QLVCLLDDQV IDSSLFNVSS
     GRKTDGHRFL GETLELASAE NYEKALKNQY VIADRQDRQE DIARQIEALC QDKNWQSPLY
     NQALLDEVTD LVEYPTVFFG EFDSSFLSVP ERILETSMAD HQRYFPVRSK LGDFLPYFIG
     VRNGNEAGLE NVVAGNEKVL VARLEDAKFF YQEDKDHSID YFLNQLDQVT YHDKLGSMQD
     KQDRVGQICL DLLDYVSLTQ AERDDLSRAA AIYKFDLVTA VVDEFSSLQG YIGGVYAQEF
     GESQAVAQAI GEQYLPTSSR GDLPESKLGS ILAMADKLES LLMFFSINLI PSGSNDPYAL
     RRAAYGLIRI LDDQDLSLDL TDFFYQLAQD LGIEDTHFIE KLDQFIKERV DKYLEAQYQI
     PHDIRQAAIS GLHLNPVKAI KVGQKLAEDR GSQDYKFMVE SLSRVANMTQ QETSHAEVDP
     DLAQSQSEED LIKASVFLLG LFQESDDITA QYEALKEISP KIEAFFDNNM VNTEDDQVRA
     NRYAILDQIT QASHSFADFN QLLTK
//
DBGET integrated database retrieval system