ID I0BPA1_9BACL Unreviewed; 484 AA.
AC I0BPA1;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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 ORFNames=B2K_26500 {ECO:0000313|EMBL:AFH64198.1};
OS Paenibacillus mucilaginosus K02.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=997761 {ECO:0000313|EMBL:AFH64198.1, ECO:0000313|Proteomes:UP000007392};
RN [1] {ECO:0000313|EMBL:AFH64198.1, ECO:0000313|Proteomes:UP000007392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K02 {ECO:0000313|EMBL:AFH64198.1,
RC ECO:0000313|Proteomes:UP000007392};
RA Xiao B., Sun L., Xiao L., Lian B.;
RT "Complete genome sequence of Paenibacillus mucilaginosus K02.";
RL Submitted (JUN-2013) 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: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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003422; AFH64198.1; -; Genomic_DNA.
DR RefSeq; WP_013919454.1; NC_017672.3.
DR AlphaFoldDB; I0BPA1; -.
DR KEGG; pmw:B2K_26500; -.
DR PATRIC; fig|997761.3.peg.5283; -.
DR HOGENOM; CLU_001882_4_2_9; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000007392; 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 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};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, 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}.
FT DOMAIN 41..289
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 484 AA; 55398 MW; 06E91A688D4B5D64 CRC64;
MAKEKQDKQF VKEITPQGED FSRWYIDVIK KADLMSYSPV RGCIVFKPDG YEIWENIQKE
LDRRFKETGH RNAYFPMFIP ESFFQKEKEH VEGFNPELPW VTEAGGEKLE ERLAIRPTSE
TMIGHMYSEW INSYRDLPVL INQWANVVRW EKRTQPFLRT SEFLWQEGHT AHEDEADARK
ETMQMLEIYR DFAENYLAIP VIMGQKTPSE KFAGAVDTYS IEAMMKDGKA VQAGTSHYLG
TNFAVAFDIK YLDRENTHQF CHTTSWGVST RLIGALIMVH GDDRGLALPP KIAPTQVVMI
PIGPPKTREA VVGRVDELYS QLKAAGVRAK VDDNPDQSPG WKFNEYEMRG VPIRVELGPR
DMENGQVVLV SRITGEKRIV QQDQFVEEVQ KLLTETHQEM YDRAKRFRDE NMTEADTVDE
LKTFLDGKRG FALSGWCGSA ACEAQVKEET GATSRNIPFE APAKPKCLVC GEPSKHTVVF
GRAY
//
