SYP_PORGI
ID SYP_PORGI Reviewed; 493 AA.
AC Q7MVS7;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01571};
DE EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01571};
DE AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01571};
DE Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01571};
GN Name=proS {ECO:0000255|HAMAP-Rule:MF_01571}; OrderedLocusNames=PG_0962;
OS Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=242619;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-308 / W83;
RX PubMed=12949112; DOI=10.1128/jb.185.18.5591-5601.2003;
RA Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J., Dewhirst F.E.,
RA Fraser C.M.;
RT "Complete genome sequence of the oral pathogenic bacterium Porphyromonas
RT gingivalis strain W83.";
RL J. Bacteriol. 185:5591-5601(2003).
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:0000255|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:0000255|HAMAP-Rule:MF_01571};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_01571}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC ProS type 3 subfamily. {ECO:0000255|HAMAP-Rule:MF_01571}.
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DR EMBL; AE015924; AAQ66092.1; -; Genomic_DNA.
DR RefSeq; WP_005874388.1; NC_002950.2.
DR AlphaFoldDB; Q7MVS7; -.
DR SMR; Q7MVS7; -.
DR STRING; 242619.PG_0962; -.
DR EnsemblBacteria; AAQ66092; AAQ66092; PG_0962.
DR KEGG; pgi:PG_0962; -.
DR PATRIC; fig|242619.8.peg.890; -.
DR eggNOG; COG0442; Bacteria.
DR HOGENOM; CLU_001882_4_2_10; -.
DR OMA; EVYWVTH; -.
DR OrthoDB; 665824at2; -.
DR BioCyc; PGIN242619:G1G02-896-MON; -.
DR Proteomes; UP000000588; 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:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00778; ProRS_core_arch_euk; 1.
DR Gene3D; 3.30.110.30; -; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 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; 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 PANTHER; PTHR43382; PTHR43382; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF09180; ProRS-C_1; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR SMART; SM00946; ProRS-C_1; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR SUPFAM; SSF64586; SSF64586; 1.
DR TIGRFAMs; TIGR00408; proS_fam_I; 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; Reference proteome.
FT CHAIN 1..493
FT /note="Proline--tRNA ligase"
FT /id="PRO_0000249147"
SQ SEQUENCE 493 AA; 56159 MW; 291675C146187136 CRC64;
MAKELKELTP RSESYSQWYQ DLVIKADLAE NSAVRGCMVI KPYGYAIWEK MQRQLDDMFK
ETGHVNAYFP LFIPKSFLSR EAEHVEGFAK ECAVVTHYRL KANPDGDGVV VDPQAKLEEE
LIVRPTSETI IWNTYKNWIQ SHRDLPILCN QWANVVRWEM RTRLFLRTAE FLWQEGHTAH
ATKEEAEEEA RRMLEVYATF AEEYMAMPVV KGVKSANERF AGAVDTYTIE ALMQDGKALQ
SGTSHFLGQN FAKAFNVTFA DKDGNRDFVW ATSWGVSTRL MGALIMSHSD DNGLVLPPKL
APYQVVIIPI YRNEEQLAQI DEKATQITQA LRAKGISVKY DNSDNKKPGW KFAEYELKGI
PVRLAMGARD LENNTIEIAR RDTLTKETVG LDGIEETVAT LLDDIQKNIF QKALNYRKEH
TITVDSYEEF KEKIEDGGFI LAHWDGTSET EERIKAETKA TIRCIPLNGD MTPGKCMVTG
KPSPQRVLFA RAY