ID   SYP_PROA2               Reviewed;         481 AA.
AC   B4S9D5;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=Paes_1587;
OS   Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=290512;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 271 / SK 413;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL   Submitted (JUN-2008) 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: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; CP001108; ACF46605.1; -; Genomic_DNA.
DR   RefSeq; WP_012506138.1; NC_011059.1.
DR   AlphaFoldDB; B4S9D5; -.
DR   SMR; B4S9D5; -.
DR   STRING; 290512.Paes_1587; -.
DR   EnsemblBacteria; ACF46605; ACF46605; Paes_1587.
DR   KEGG; paa:Paes_1587; -.
DR   eggNOG; COG0442; Bacteria.
DR   HOGENOM; CLU_001882_4_2_10; -.
DR   OMA; EVYWVTH; -.
DR   OrthoDB; 665824at2; -.
DR   Proteomes; UP000002725; 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; 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   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   PRINTS; PR01046; TRNASYNTHPRO.
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..481
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_1000215572"
SQ   SEQUENCE   481 AA;  54378 MW;  FF1D3546221758DE CRC64;
     MAEKITLRET DYSQWYIDLV RSAKLADYSD VRGCMIIRPN GYAIWEKMQA ALDAMFKATG
     HVNAYFPLFI PESFIKKEAE HIEGFAPECA VVTHGGGEQL AENLYVRPTS ETIIWSSYKK
     WIQSYRDLPI LINQWANVVR WEMRTRLFLR TTEFLWQEGH TAHATSTEAQ EEVMRMINVY
     KTFAEEYMAL PVIMGRKTES EKFAGAVETW CIEAMMQDKK ALQAGTSHNL GQNFAKAFDC
     RFQSKEGALE YVWATSWGVS TRLIGALIMA HSDDRGLVLP PKLATRQVVI IPILKGDISA
     VIEKARSIAA ELNQKGIAAF VDDSDQNSPG WKFAEYELQG IPVRLELGPR DIQSSTCIAA
     RRDTGEKSKL QLDSSLADQI NSLLESIQTN LFNRALSFRE KHTLEVSSYS EFKANIDNGF
     LVAHWDGTDE TEAKIKEETK ATIRVMPADP EMVLRYGMDQ PGTCIYSGKP STRKVIFAKA
     Y