ID A9NEY8_ACHLI Unreviewed; 474 AA.
AC A9NEY8;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01571};
DE EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01571};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01571};
DE Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01571};
GN Name=proS {ECO:0000256|HAMAP-Rule:MF_01571,
GN ECO:0000313|EMBL:ABX80918.1};
GN OrderedLocusNames=ACL_0296 {ECO:0000313|EMBL:ABX80918.1};
OS Acholeplasma laidlawii (strain PG-8A).
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Acholeplasma.
OX NCBI_TaxID=441768 {ECO:0000313|EMBL:ABX80918.1, ECO:0000313|Proteomes:UP000008558};
RN [1] {ECO:0000313|EMBL:ABX80918.1, ECO:0000313|Proteomes:UP000008558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG-8A {ECO:0000313|EMBL:ABX80918.1,
RC ECO:0000313|Proteomes:UP000008558};
RX PubMed=21784942; DOI=10.1128/JB.05059-11;
RA Lazarev V.N., Levitskii S.A., Basovskii Y.I., Chukin M.M., Akopian T.A.,
RA Vereshchagin V.V., Kostrjukova E.S., Kovaleva G.Y., Kazanov M.D.,
RA Malko D.B., Vitreschak A.G., Sernova N.V., Gelfand M.S., Demina I.A.,
RA Serebryakova M.V., Galyamina M.A., Vtyurin N.N., Rogov S.I., Alexeev D.G.,
RA Ladygina V.G., Govorun V.M.;
RT "Complete genome and proteome of Acholeplasma laidlawii.";
RL J. Bacteriol. 193:4943-4953(2011).
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:0000256|HAMAP-
CC Rule:MF_01571}.
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:0000256|ARBA:ARBA00000857,
CC ECO:0000256|HAMAP-Rule:MF_01571};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571}.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC anticodon-binding domain and the C-terminal extension.
CC {ECO:0000256|HAMAP-Rule:MF_01571}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 3 subfamily. {ECO:0000256|HAMAP-Rule:MF_01571}.
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DR EMBL; CP000896; ABX80918.1; -; Genomic_DNA.
DR RefSeq; WP_012242249.1; NC_010163.1.
DR AlphaFoldDB; A9NEY8; -.
DR STRING; 441768.ACL_0296; -.
DR GeneID; 66293292; -.
DR KEGG; acl:ACL_0296; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_001882_4_2_14; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000008558; 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; cd00862; ProRS_anticodon_zinc; 1.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR Gene3D; 3.30.110.30; C-terminal domain of ProRS; 1.
DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 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; IPR004499; Pro-tRNA-ligase_IIa_arc-type.
DR InterPro; IPR016061; Pro-tRNA_ligase_II_C.
DR InterPro; IPR017449; Pro-tRNA_synth_II.
DR InterPro; IPR033721; ProRS_core_arch_euk.
DR NCBIfam; TIGR00408; proS_fam_I; 1.
DR PANTHER; PTHR43382:SF2; BIFUNCTIONAL GLUTAMATE_PROLINE--TRNA LIGASE; 1.
DR PANTHER; PTHR43382; PROLYL-TRNA SYNTHETASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SMART; SM00946; ProRS-C_1; 1.
DR SUPFAM; SSF64586; C-terminal domain of ProRS; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_01571};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01571}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01571};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01571};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01571};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01571}; Reference proteome {ECO:0000313|Proteomes:UP000008558}.
FT DOMAIN 43..286
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 474 AA; 54253 MW; 0D2096C9E6BC7204 CRC64;
MSKNKKLVES ITSRDVDFSQ WYTDLCLKAE LMDYSNTQGF IIYRPLGYGI WENIQNYLNN
EFRKTGHQNV YMPMLIPESL FQKEKDHVSG FAPETAMVTT TGVENLSERL IIRPTSEVLF
GTHYSKIVKS YRDLPKMYNQ WCSVVRWEKT TRPFLRGKEF LWQEGHTVHA TAEEAKKETH
QMLEVYDKLG KELLAIPFVT GRKTDKEKFA GALETYAIEA LMHDGQALQS GTSHYFGNEF
AHAFDIKFLN DKNELEYAYQ TSWGVSTRLI GAIIMVHGDD NGLVLPPYVA PTQVVIVPIR
PNEEVLSAVK QIENELSDKF RVFVDDSDKS PGWKFSEHEM KGVPLRIEIG PRDLENGQVV
VTFRHNYEKH TVALTDLHKF VEDGLKTMHE AMYQKALEAT TSRTYEAKSY DEFKAFLKQG
GYIKMSTCGE EAEIQIKEET GATARVILDE PLLTENCPVT GKKATQTILF ARAY
//
