ID SYP_ACESD Reviewed; 481 AA.
AC Q9L4Q8; E3PU03;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=Proline--tRNA ligase;
DE EC=6.1.1.15;
DE AltName: Full=Prolyl-tRNA synthetase;
DE Short=ProRS;
GN Name=proS; OrderedLocusNames=CLOST_2239;
OS Acetoanaerobium sticklandii (strain ATCC 12662 / DSM 519 / JCM 1433 / CCUG
OS 9281 / NCIMB 10654 / HF) (Clostridium sticklandii).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Acetoanaerobium.
OX NCBI_TaxID=499177;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=10085076; DOI=10.1074/jbc.274.13.8445;
RA Kabisch U.C., Graentzdoerffer A., Schierhorn A., Ruecknagel K.P.,
RA Andreesen J.R., Pich A.;
RT "Identification of D-proline reductase from Clostridium sticklandii as a
RT selenoenzyme and indications for a catalytically active pyruvoyl group
RT derived from a cysteine residue by cleavage of a proprotein.";
RL J. Biol. Chem. 274:8445-8454(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12662 / DSM 519 / JCM 1433 / CCUG 9281 / NCIMB 10654 / HF;
RX PubMed=20937090; DOI=10.1186/1471-2164-11-555;
RA Fonknechten N., Chaussonnerie S., Tricot S., Lajus A., Andreesen J.R.,
RA Perchat N., Pelletier E., Gouyvenoux M., Barbe V., Salanoubat M.,
RA Le Paslier D., Weissenbach J., Cohen G.N., Kreimeyer A.;
RT "Clostridium sticklandii, a specialist in amino acid degradation:revisiting
RT its metabolism through its genome sequence.";
RL BMC Genomics 11:555-555(2010).
RN [3]
RP PROLINE AND CYSTEINE ACTIVATION, LACK OF EDITING ACTIVITY, AND KINETIC
RP PARAMETERS.
RX PubMed=12130657; DOI=10.1074/jbc.m206928200;
RA Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H.,
RA Hartsch T., Soell D.;
RT "Cysteine activation is an inherent in vitro property of prolyl-tRNA
RT synthetases.";
RL J. Biol. Chem. 277:34743-34748(2002).
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). Can inadvertently
CC accommodate and process cysteine. Misacylated Cys-tRNA(Pro) is not
CC edited by ProRS; this function may be provided by ProX.
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;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.05 mM for proline {ECO:0000269|PubMed:12130657};
CC KM=0.01 mM for cysteine {ECO:0000269|PubMed:12130657};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC anticodon-binding domain and the C-terminal extension. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 3 subfamily. {ECO:0000305}.
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DR EMBL; AJ130879; CAB71307.1; -; Genomic_DNA.
DR EMBL; FP565809; CBH22357.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9L4Q8; -.
DR SMR; Q9L4Q8; -.
DR STRING; 1511.CLOST_2239; -.
DR KEGG; cst:CLOST_2239; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_001882_4_2_9; -.
DR SABIO-RK; Q9L4Q8; -.
DR Proteomes; UP000007041; 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:0016740; F:transferase activity; IEA:UniProt.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..481
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000139328"
SQ SEQUENCE 481 AA; 55145 MW; 9D04371CC0056123 CRC64;
MAKKDQEFVK DITNMDEDFP QWYTDVITKT DLVDYSPVKG FMVIKPYGYA IWENIQAFLD
RRFKETGHQN CYFPLLIPES LLNKEKEHVE GFAPEVAWVT HGGSEKLAER LCVRPTSETI
ICSMYSKWLT SYRELPYLYN QWCSVVRWEK STRPFLRTSE FLWQEGHTLH ETAEEAQAET
LQMLAIYKEM AEDLLAIPVV DGRKSDRERF AGAAATYTIE ALMHDGKALQ SGTSHNLAQH
FTKAFDITFQ GRTGELEYPH HTSWGASTRL IGGIIMVHGD NRGLVLPPRV APTQVVIIPI
AQNKEGVLDK AYEIKKELEA KGIRVTLDDD TNYSPGWKFN QYEMKGVPLR LEIGPRDIEN
NVAMIARRDT LSKDSYSLDN IGDTVKNLLD TVHTDMLERA RAHRDSKTFT FKDYEEFKRK
MIETPGFAKG MWCGEEECEA KIKEDTGVTI RCIPFVQENL GETCQFCGKP AKHMVYLAKA
Y
//
