SYP_SULSY
ID SYP_SULSY Reviewed; 564 AA.
AC B2V6W5;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01569};
GN OrderedLocusNames=SYO3AOP1_1699;
OS Sulfurihydrogenibium sp. (strain YO3AOP1).
OC Bacteria; Aquificae; Aquificales; Hydrogenothermaceae;
OC Sulfurihydrogenibium; unclassified Sulfurihydrogenibium.
OX NCBI_TaxID=436114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YO3AOP1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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:0000255|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:0000255|HAMAP-Rule:MF_01569};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01569}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}.
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DR EMBL; CP001080; ACD67297.1; -; Genomic_DNA.
DR RefSeq; WP_012460353.1; NC_010730.1.
DR AlphaFoldDB; B2V6W5; -.
DR SMR; B2V6W5; -.
DR STRING; 436114.SYO3AOP1_1699; -.
DR EnsemblBacteria; ACD67297; ACD67297; SYO3AOP1_1699.
DR KEGG; sul:SYO3AOP1_1699; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_016739_0_0_0; -.
DR OMA; NCDYAAN; -.
DR OrthoDB; 665824at2; -.
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:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00861; ProRS_anticodon_short; 1.
DR CDD; cd00779; ProRS_core_prok; 1.
DR Gene3D; 3.30.930.10; -; 2.
DR Gene3D; 3.40.50.800; -; 1.
DR Gene3D; 3.90.960.10; -; 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 Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF04073; tRNA_edit; 1.
DR PRINTS; PR01046; TRNASYNTHPRO.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF55826; SSF55826; 1.
DR TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..564
FT /note="Proline--tRNA ligase"
FT /id="PRO_1000199431"
SQ SEQUENCE 564 AA; 63953 MW; 87D776D1BA3B4163 CRC64;
MLASKFFMPT LKENPSDAVV PSHIYLVRGG FIRSLSAGIY EYLPLGLKVL RKIENIIRKH
MDDSGALEVL LPILTPAELW KETGRWHVYG KELFRLKDRK DAEFALGPTH EETITDLVRK
NVRSYKDLPL NFYQIQTKFR DEARPRYGLI RGREFIMKDG YSFDVSEEDA KKTYEVMKEA
YHKIFKELGL DYLMVEADVG AIGGKFSHEF VVKVPSGEAH IVYCEKCGYA ANVEAAKFHH
HKLPPEEPKP IEKVYTPDIK SVEDVANFLN VPLTKLVKTL IYKIDDKDFV AVLIRGDREL
NETKLANLFK AIDVRMATKE ELESLGIPEG FVGPIGLNLP IYADFSLKEL YNIVVGANEK
DYHYINANID RDFKVSGFYD LATAKEGDPC PVCHLPLKET TGLEVGHIFL LGTKYSESMK
AYFVDKDGKE KSIIMGCYGI GVSRLISAIV EQYHDDKGII WPENLAPFNV HILVLNPKDQ
ESLNVGFDIY KKLKEKGLDV LLDERDESAG AKFKDADLIG IPHRIVIGKA LKEGKVEYQK
RDGSIKELVD VKLIINKLMD GYHG