ID   SYP_CERS4               Reviewed;         445 AA.
AC   Q3IZS9;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01570};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01570};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01570};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01570};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01570}; OrderedLocusNames=RHOS4_23870;
GN   ORFNames=RSP_0778;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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_01570}.
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_01570};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01570}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01570}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01570}.
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DR   EMBL; CP000143; ABA79955.1; -; Genomic_DNA.
DR   RefSeq; WP_011338481.1; NZ_CP030271.1.
DR   RefSeq; YP_353856.1; NC_007493.2.
DR   AlphaFoldDB; Q3IZS9; -.
DR   SMR; Q3IZS9; -.
DR   STRING; 272943.RSP_0778; -.
DR   EnsemblBacteria; ABA79955; ABA79955; RSP_0778.
DR   KEGG; rsp:RSP_0778; -.
DR   PATRIC; fig|272943.9.peg.2735; -.
DR   eggNOG; COG0442; Bacteria.
DR   OMA; NCDYAAN; -.
DR   PhylomeDB; Q3IZS9; -.
DR   Proteomes; UP000002703; Chromosome 1.
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; cd00861; ProRS_anticodon_short; 1.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   HAMAP; MF_01570; Pro_tRNA_synth_type2; 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; IPR023716; Prolyl-tRNA_ligase_IIa_type2.
DR   InterPro; IPR044140; ProRS_anticodon_short.
DR   InterPro; IPR033730; ProRS_core_prok.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF55681; SSF55681; 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..445
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000248913"
SQ   SEQUENCE   445 AA;  50421 MW;  988BB31B6019516C CRC64;
     MRLSRYFLPV LKENPSEAQI VSHRYMLRAG MIKQQAAGIY SWLPLGFKVL KRIEQIVHEE
     QIRAGHIPLL MPTLQPADLW RESGRYDDYG EEMLRITDRH KRDMLYGPTN EEMITDIFRS
     HVSSYKDLPL TLYHIQWKFR DEIRPRFGVM RGREFLMKDG YNFDLDYESA IHAYNRHMVS
     YLRTYERMGL QAIPMRAASG PIGGDNTHEF LVLASTGESE VFYDAAITDL KFGDRVVNYD
     DRAECEAIVK EWTAPYARTD ETHDEAVFGQ IPEERRRSSR GIEVGQIFYF GTKYSEPMGA
     NVVTADGSRV PVHMGSHGIG VSRLLGAIIE ASHDDKGIIW PEGVTPFHAG IVNLKQGDSS
     TDLACEALYR DLSARGLEPL YDDRDERAGA KFATMDLIGL PWRITVGPRG ISAGKVELTN
     RRTGESEEMS SGAAVDRLAQ IYAGI