SYS_KLEP7
ID SYS_KLEP7 Reviewed; 430 AA.
AC A6T6Z0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Serine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00176};
DE EC=6.1.1.11 {ECO:0000255|HAMAP-Rule:MF_00176};
DE AltName: Full=Seryl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
DE Short=SerRS {ECO:0000255|HAMAP-Rule:MF_00176};
DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase {ECO:0000255|HAMAP-Rule:MF_00176};
GN Name=serS {ECO:0000255|HAMAP-Rule:MF_00176};
GN OrderedLocusNames=KPN78578_09000; ORFNames=KPN_00925;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able
CC to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-
CC seryl-tRNA(Sec), which will be further converted into selenocysteinyl-
CC tRNA(Sec). {ECO:0000255|HAMAP-Rule:MF_00176}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669,
CC Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00176};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-serine + tRNA(Sec) = AMP + diphosphate + H(+) + L-
CC seryl-tRNA(Sec); Xref=Rhea:RHEA:42580, Rhea:RHEA-COMP:9742,
CC Rhea:RHEA-COMP:10128, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00176};
CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00176}.
CC -!- SUBUNIT: Homodimer. The tRNA molecule binds across the dimer.
CC {ECO:0000255|HAMAP-Rule:MF_00176}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00176}.
CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a N-
CC terminal extension that is involved in tRNA binding.
CC {ECO:0000255|HAMAP-Rule:MF_00176}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type-1 seryl-tRNA synthetase subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00176}.
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DR EMBL; CP000647; ABR76361.1; -; Genomic_DNA.
DR RefSeq; WP_002898139.1; NC_009648.1.
DR PDB; 6HHY; X-ray; 2.27 A; A=1-430.
DR PDB; 6HHZ; X-ray; 2.15 A; A=1-430.
DR PDB; 6HI0; X-ray; 2.25 A; A=1-430.
DR PDB; 6S30; X-ray; 2.41 A; A=1-430.
DR PDB; 7AP1; X-ray; 2.18 A; A=1-430.
DR PDBsum; 6HHY; -.
DR PDBsum; 6HHZ; -.
DR PDBsum; 6HI0; -.
DR PDBsum; 6S30; -.
DR PDBsum; 7AP1; -.
DR AlphaFoldDB; A6T6Z0; -.
DR SMR; A6T6Z0; -.
DR STRING; 272620.KPN_00925; -.
DR jPOST; A6T6Z0; -.
DR PRIDE; A6T6Z0; -.
DR EnsemblBacteria; ABR76361; ABR76361; KPN_00925.
DR KEGG; kpn:KPN_00925; -.
DR HOGENOM; CLU_023797_1_1_6; -.
DR OMA; SPCFRRE; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000000265; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00770; SerRS_core; 1.
DR Gene3D; 1.10.287.40; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00176; Ser_tRNA_synth_type1; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002317; Ser-tRNA-ligase_type_1.
DR InterPro; IPR015866; Ser-tRNA-synth_1_N.
DR InterPro; IPR042103; SerRS_1_N_sf.
DR InterPro; IPR033729; SerRS_core.
DR InterPro; IPR010978; tRNA-bd_arm.
DR PANTHER; PTHR43697; PTHR43697; 1.
DR Pfam; PF02403; Seryl_tRNA_N; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001529; Ser-tRNA-synth_IIa; 1.
DR PRINTS; PR00981; TRNASYNTHSER.
DR SUPFAM; SSF46589; SSF46589; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00414; serS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..430
FT /note="Serine--tRNA ligase"
FT /id="PRO_1000019705"
FT BINDING 237..239
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 268..270
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 291
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 355..358
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 391
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:6HHZ"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 27..62
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 69..100
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 168..186
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 201..206
FT /evidence="ECO:0007829|PDB:6HHZ"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:6HHZ"
FT TURN 227..229
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 232..234
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 250..252
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 258..267
FT /evidence="ECO:0007829|PDB:6HHZ"
FT TURN 274..277
FT /evidence="ECO:0007829|PDB:6HI0"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 285..296
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 298..300
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 301..318
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 323..327
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 330..332
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 338..347
FT /evidence="ECO:0007829|PDB:6HHZ"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 352..363
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 365..370
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:6HHZ"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:6S30"
FT STRAND 386..394
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 395..405
FT /evidence="ECO:0007829|PDB:6HHZ"
FT HELIX 417..423
FT /evidence="ECO:0007829|PDB:6HHZ"
SQ SEQUENCE 430 AA; 48603 MW; 621A4ECF429A4F07 CRC64;
MLDPNLLRTE PDAVAEKLAR RGFKLDVDKL RALEERRKVL QVQTENLQAE RNSRSKSIGQ
AKARGEDIEP LRLEVNKLGE QLDAAKSELE TLLAEIRDIA LAIPNIPHDD VPVGRDENDN
VEVSRWGTPR QFDFEVRDHV TLGEMHGGLD FAAAVKLTGS RFVVMKGQLA RLHRALAQFM
LDLHTEQHGY SENYVPYLVN QDTLYGTGQL PKFAGDLFHT RPLEEEADSS NYALIPTAEV
PLTNLVRDEI IDEDDLPIKM TAHTPCFRSE AGSYGRDTRG LIRMHQFDKV EMVQIVRPED
SMAALEEMTG HAEKVLQLLG LPYRKVALCT GDMGFSACKT YDLEVWVPAQ NTYREISSCS
NVWDFQARRM QARCRSKSDK KTRLVHTLNG SGLAVGRTLV ALMENYQQAD GRIEIPEVLR
PYMRGLEYIG
