ID F8IIP8_ALIAT Unreviewed; 483 AA.
AC F8IIP8;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
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:AEJ44573.1};
GN OrderedLocusNames=TC41_2679 {ECO:0000313|EMBL:AEJ44573.1};
OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ44573.1, ECO:0000313|Proteomes:UP000000292};
RN [1] {ECO:0000313|EMBL:AEJ44573.1, ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|EMBL:AEJ44573.1,
RC ECO:0000313|Proteomes:UP000000292};
RX PubMed=21914900; DOI=10.1128/JB.05709-11;
RA Chen Y., He Y., Zhang B., Yang J., Li W., Dong Z., Hu S.;
RT "Complete Genome Sequence of Alicyclobacillus acidocaldarius Strain Tc-
RT 4-1.";
RL J. Bacteriol. 193:5602-5603(2011).
RN [2] {ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292};
RA Chen Y., He Y., Dong Z., Hu S.;
RT "The complete genome sequence of Alicyclobacillus acidocaldarius sp. Tc-4-
RT 1.";
RL Submitted (JUN-2011) 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}.
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DR EMBL; CP002902; AEJ44573.1; -; Genomic_DNA.
DR RefSeq; WP_014465402.1; NC_017167.1.
DR AlphaFoldDB; F8IIP8; -.
DR STRING; 1048834.TC41_2679; -.
DR KEGG; aad:TC41_2679; -.
DR PATRIC; fig|1048834.4.peg.2537; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_001882_4_2_9; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000000292; 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 39..287
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 483 AA; 55273 MW; 390B8503FC8F948B CRC64;
MAKQDKQFVK EITPQSEDFS RWYIDVLQKA EWMDYAPVRG CIVIRPDAYE IWERCQRELD
REFKRTGHRN AYFPLFIPES FFEKEKEHVE GFNPELPWVT EAGGDILEER LAVRPTSETM
FGHMYAQWIQ SYRDLPLLLN QWANVVRWEK RTLPFLRTSE FLWQEGHTAH ATEEEAREET
MRMLGIYADF VESFLAIPVI RGQKTPSEKF AGAVETYTIE SLMKDGRALQ TATSHYLGQN
FAKSFEIQYL DKDNQLKYVY TTSWGMSTRI LGAIVMVHGD DRGLVLPPKL APTQVVVVPI
GPAKAREAVV AKARELFDAL KRADIRVHLD DRDDVSPGWK FNEYELRGVP IRLELGPRDL
EASQAVLARR DTGEKITVPL DAVVERVQAL LSDIQRDLFQ AAKRRLEENS HVAETLDQLV
EIIQTKRGFV LAGWCGDDAC ERAVKDACTA TSRCIPFNPP ARPATCVTCG KPAAHAVWFA
KSY
//
