SYP_RHOP2
ID SYP_RHOP2 Reviewed; 439 AA.
AC Q2IWW0;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01570};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01570};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01570};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01570};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01570}; OrderedLocusNames=RPB_2597;
OS Rhodopseudomonas palustris (strain HaA2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HaA2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Pelletier D.A.,
RA Kyrpides N., Anderson I., Oda Y., Harwood C.S., Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris HaA2.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC step reaction: proline is first activated by ATP to form Pro-AMP and
CC then transferred to the acceptor end of tRNA(Pro). {ECO:0000255|HAMAP-
CC Rule:MF_01570}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC EC=6.1.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01570};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01570}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01570}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01570}.
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DR EMBL; CP000250; ABD07300.1; -; Genomic_DNA.
DR RefSeq; WP_011441485.1; NC_007778.1.
DR AlphaFoldDB; Q2IWW0; -.
DR SMR; Q2IWW0; -.
DR STRING; 316058.RPB_2597; -.
DR PRIDE; Q2IWW0; -.
DR EnsemblBacteria; ABD07300; ABD07300; RPB_2597.
DR KEGG; rpb:RPB_2597; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_4_2_5; -.
DR OMA; NCDYAAN; -.
DR OrthoDB; 665824at2; -.
DR Proteomes; UP000008809; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_01570; Pro_tRNA_synth_type2; 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; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR InterPro; IPR023716; Prolyl-tRNA_ligase_IIa_type2.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..439
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000248910"
SQ SEQUENCE 439 AA; 49301 MW; F6B06365AEFECB54 CRC64;
MRLSRFFLPI LKENPKEAEI VSHRLMLRAG MLRQEAAGIY AWLPLGHRVL KKIEQIVREE
QNRAGAIELL MPTLQLADLW RESGRYDAYG PEMLRISDRH KRELLYGPTN EEMITEIFRA
YVKSYKSLPL NLYHIQWKFR DEQRPRFGVM RGREFLMKDA YSFDVDEAAA RKSYNRMFVA
YLRTFARMGL KAIPMRAETG PIGGDLSHEF IVLAETGESG VYCDRDVLSL PVPDETVDYD
GDLTPIIKQW TSVYAATEDV HDAVRYESEV PEANRLHTRG IEVGQIFYFG TKYSDSMKAN
VAGPDGTDAP IHGGSYGVGV SRLVGAIIEA CHDDNGIIWP EEVAPFRVAI LNLKQGDAAT
DAACEQLYKE LAAKGVDVLY DDTDQRAGAK FATADLIGIP WQVLVGPKGL ADGKIELKRR
SDGSRENIAL AETVARLAP