ID D9TRS9_THETC Unreviewed; 570 AA.
AC D9TRS9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Proline--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01569};
DE EC=6.1.1.15 {ECO:0000256|HAMAP-Rule:MF_01569};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01569};
DE Short=ProRS {ECO:0000256|HAMAP-Rule:MF_01569};
GN Name=proS {ECO:0000256|HAMAP-Rule:MF_01569};
GN OrderedLocusNames=Tthe_0407 {ECO:0000313|EMBL:ADL67976.1};
OS Thermoanaerobacterium thermosaccharolyticum (strain ATCC 7956 / DSM 571 /
OS NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM 00135 / 2032) (Clostridium
OS thermosaccharolyticum).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Thermoanaerobacterium.
OX NCBI_TaxID=580327 {ECO:0000313|EMBL:ADL67976.1, ECO:0000313|Proteomes:UP000001626};
RN [1] {ECO:0000313|EMBL:ADL67976.1, ECO:0000313|Proteomes:UP000001626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7956 / DSM 571 / NCIMB 9385 / NCA 3814 / NCTC 13789 / WDCM
RC 00135 / 2032 {ECO:0000313|Proteomes:UP000001626};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N., Mikhailova N.,
RA Hemme C.L., Woyke T.;
RT "Complete sequence of Thermoanaerobacterium thermosaccharolyticum DSM
RT 571.";
RL Submitted (AUG-2010) 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). As ProRS can
CC inadvertently accommodate and process non-cognate amino acids such as
CC alanine and cysteine, to avoid such errors it has two additional
CC distinct editing activities against alanine. One activity is designated
CC as 'pretransfer' editing and involves the tRNA(Pro)-independent
CC hydrolysis of activated Ala-AMP. The other activity is designated
CC 'posttransfer' editing and involves deacylation of mischarged Ala-
CC tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
CC {ECO:0000256|HAMAP-Rule:MF_01569}.
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_01569};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01569}.
CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC editing domain and the C-terminal anticodon-binding domain.
CC {ECO:0000256|HAMAP-Rule:MF_01569}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 1 subfamily. {ECO:0000256|HAMAP-Rule:MF_01569}.
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DR EMBL; CP002171; ADL67976.1; -; Genomic_DNA.
DR RefSeq; WP_013296952.1; NC_014410.1.
DR AlphaFoldDB; D9TRS9; -.
DR STRING; 580327.Tthe_0407; -.
DR KEGG; ttm:Tthe_0407; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_0_0_9; -.
DR OrthoDB; 9809052at2; -.
DR Proteomes; UP000001626; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
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; cd04334; ProRS-INS; 1.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_01569; Pro_tRNA_synth_type1; 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; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR InterPro; IPR044140; ProRS_anticodon_short.
DR InterPro; IPR033730; ProRS_core_prok.
DR InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR NCBIfam; TIGR00409; proS_fam_II; 1.
DR PANTHER; PTHR42753; MITOCHONDRIAL RIBOSOME PROTEIN L39/PROLYL-TRNA LIGASE FAMILY MEMBER; 1.
DR PANTHER; PTHR42753:SF2; PROLINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF04073; tRNA_edit; 1.
DR PIRSF; PIRSF001535; ProRS_1; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF55826; YbaK/ProRS associated domain; 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_01569};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01569};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01569};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01569};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01569};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01569}; Reference proteome {ECO:0000313|Proteomes:UP000001626}.
FT DOMAIN 38..466
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 570 AA; 64144 MW; C84F107222FDADD3 CRC64;
MRLSQLLIPT LREVPAEAEI PSHTLMLKAA MMRKLASGVY IYLPLGKRVL KKIEEIVREE
MDRAGAQEVL MPAIIPAELL KESGRWDVFG PEMFKLKDRN DREFCLGPTH EEVFTDLVRN
EVKSYRQLPL TIYQIQTKYR DERRPRFGVM RSREFIMKDA YSFDVDWDGL DASFDKMYDA
YCRIFDRCGL KYTVVEADSG AMGGKDSKEF MVTSSVGEAV IAYCDSCGYA ANEEKAECTV
EHKSDEEIKP LEKIYTPDVR TIDELVSYLD VKSDKFVKTL IYTYKDKVAA VLLRGDREVN
TVKLANLLKV NENDIDFADE ETVRSVTGAN VGFAGPIGLK GDVLLIADAE VPMMKNIIVG
ANETDYHLKN TNYGRDFKAD VVSDIRKVVD GDKCPRCGNP LKLERGIEVG HIFKLGTKYS
DALGANYIDE NGNEKPMIMG CYGIGLNRIA AAAIEQNHDD KGIIWPMSIA PYHAIVVPVN
VSNDAQRNLA EKIYDELSKA GIETLIDDRD LRAGVKFNDA DLLGIPIRIT VGKKASDNIV
ELKLRRDENS IELNYDEVVN KVKELIINSI
//
