SYS_PSEAE
ID SYS_PSEAE Reviewed; 426 AA.
AC Q9I0M6;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
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}; OrderedLocusNames=PA2612;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG06000.1; -; Genomic_DNA.
DR PIR; G83320; G83320.
DR RefSeq; NP_251302.1; NC_002516.2.
DR RefSeq; WP_003097631.1; NZ_QZGE01000008.1.
DR PDB; 6HDZ; X-ray; 2.06 A; A/B=1-426.
DR PDB; 6HE1; X-ray; 2.22 A; A/B=1-426.
DR PDB; 6HE3; X-ray; 2.16 A; A/B=1-426.
DR PDBsum; 6HDZ; -.
DR PDBsum; 6HE1; -.
DR PDBsum; 6HE3; -.
DR AlphaFoldDB; Q9I0M6; -.
DR SMR; Q9I0M6; -.
DR STRING; 287.DR97_5350; -.
DR PaxDb; Q9I0M6; -.
DR PRIDE; Q9I0M6; -.
DR EnsemblBacteria; AAG06000; AAG06000; PA2612.
DR GeneID; 882318; -.
DR KEGG; pae:PA2612; -.
DR PATRIC; fig|208964.12.peg.2733; -.
DR PseudoCAP; PA2612; -.
DR HOGENOM; CLU_023797_1_1_6; -.
DR InParanoid; Q9I0M6; -.
DR OMA; SPCFRRE; -.
DR PhylomeDB; Q9I0M6; -.
DR BioCyc; PAER208964:G1FZ6-2652-MON; -.
DR UniPathway; UPA00906; UER00895.
DR Proteomes; UP000002438; 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..426
FT /note="Serine--tRNA ligase"
FT /id="PRO_0000122101"
FT BINDING 233..235
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 264..266
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 287
FT /ligand="L-serine"
FT /ligand_id="ChEBI:CHEBI:33384"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 351..354
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00176"
FT BINDING 387
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:6HDZ"
FT HELIX 11..19
FT /evidence="ECO:0007829|PDB:6HDZ"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 27..63
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 69..100
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 117..119
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 139..144
FT /evidence="ECO:0007829|PDB:6HDZ"
FT TURN 145..147
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 167..187
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:6HDZ"
FT TURN 210..213
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 234..239
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 240..242
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 249..251
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 275..279
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 281..292
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 294..296
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 297..314
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 319..323
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 334..342
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 344..346
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 347..359
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 361..366
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6HDZ"
FT TURN 373..375
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:6HDZ"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 391..401
FT /evidence="ECO:0007829|PDB:6HDZ"
FT HELIX 413..418
FT /evidence="ECO:0007829|PDB:6HDZ"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:6HDZ"
SQ SEQUENCE 426 AA; 47232 MW; 03913971C1369C06 CRC64;
MLDPKLVRTQ PQEVAARLAT RGFQLDVARI EALEEQRKSV QTRTEQLQAE RNARSKAIGQ
AKQRGEDIAP LLADVDRMGS ELEEGKRQLD AIQGELDAML LGIPNLPHES VPVGADEDAN
VEVRRWGTPK TFDFEVKDHV ALGERHGWLD FETAAKLSGA RFALMRGPIA RLHRALAQFM
INLHTAEHGY EEAYTPYLVQ APALQGTGQL PKFEEDLFKI GRDGEADLYL IPTAEVSLTN
IVSGQILDAK QLPLKFVAHT PCFRSEAGAS GRDTRGMIRQ HQFDKVEMVQ IVDPATSYEA
LEGLTANAER VLQLLELPYR VLALCTGDMG FGATKTYDLE VWVPSQDKYR EISSCSNCGD
FQARRMQARY RNPETGKPEL VHTLNGSGLA VGRTLVAVLE NYQQADGSIR VPEVLKPYMA
GIEVIG
